F0F1 ATP synthase subunit C - STRING protein network

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organism

protein

Achromobacter arsenitoxydans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. KYC_24767, EHK63541.1, 359361792, F0F1 ATP synthase subunit C]

Achromobacter insuavis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AXXA_12512, EGP46112.1, 32054238, F0F1 ATP synthase subunit C]

Achromobacter piechaudii HLE

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. QWC_27052, EJO28402.1, J4P3W2, F0F1 ATP synthase subunit C]

Acidovorax sp. KKS102

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C380_01985, AFU44123.1, WP_015012210.1, F0F1 ATP synthase subunit C]

Acinetobacter sp. HR7

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GW12_20870, KGT46904.1, KGT46904, F0F1 ATP synthase subunit C]

Actibacterium atlanticum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ATO10_12244, KCV81376.1, A0A058ZKN9, F0F1 ATP synthase subunit C]

Actinobacillus minor NM305

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AM305_02493, EER46237.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Actinobacillus suis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ASU2_09325, AFU19995.1, asi:ASU2_09325, F0F1 ATP synthase subunit C]

Advenella kashmirensis W13003

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. W822_11050, ETF03323.1, WP_014749574.1, F0F1 ATP synthase subunit C]

Aeromonas diversa

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. G114_08260, ENY72367.1, N9VAU0_9GAMM, F0F1 ATP synthase subunit C]

Aeromonas hydrophila ATCC7966

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AHA_4267, ABK37785.1, GI:117560837, F0F1 ATP synthase subunit C]

Aeromonas salmonicida

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ASA_4355, ABO92270.1, 4998490, F0F1 ATP synthase subunit C]

Afipia sp. P5210

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. X566_05830, ETR77190.1, W3RJA6_9BRAD, F0F1 ATP synthase subunit C]

Aggregatibacter actinomycetemcomitans D7S1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RO04_06240, ACT75_06085, D7S_01237, F0F1 ATP synthase subunit C]

Aggregatibacter actinomycetemcomitans RhAA1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RHAA1_02546, EHK90645.1, WP_005539567.1, F0F1 ATP synthase subunit C]

Agrobacterium albertimagni

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. QWE_13208, EKF59214.1, K2Q676, F0F1 ATP synthase subunit C]

Agrobacterium tumefaciens CCNWGS0286

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AWN88_23225, BV900_06315, A6U97_06785, F0F1 ATP synthase subunit C]

Agrobacterium tumefaciens Cherry

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H009_08221, EMS98169.1, EMS98169, F0F1 ATP synthase subunit C]

Alcanivorax hongdengensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A11A3_14552, EKF73248.1, 407764782, F0F1 ATP synthase subunit C]

Alcanivorax sp. P2S70

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Q670_03370, ERP89438.1, WP_007151035.1, F0F1 ATP synthase subunit C]

Alicyclobacillus acidoterrestris

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N007_08845, EPZ45540.1, EPZ45540, F0F1 ATP synthase subunit C]

Alishewanella jeotgali

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AJE_08987, EHR40976.1, H3ZEL3_9ALTE, F0F1 ATP synthase subunit C]

Alteromonas macleodii Black

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AMBLS11_18955, AFT80352.1, K0D9Z3_ALTMS, F0F1 ATP synthase subunit C]

Alteromonas macleodii Deep

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BM525_18540, AEB00219.1, MADE_1020480, F0F1 ATP synthase subunit C]

Alteromonas sp. SN2

ambt_07075 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AEF02948.1, F5Z7A5_ALTNA, F0F1 ATP synthase subunit C]

Alteromonas sp. SN2

ambt_22175 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AEF05920.1, F5ZGF2, F0F1 ATP synthase subunit C]

Anoxybacillus flavithermus AK1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. TAF16_0393, CA592_09745, B4168_3784, F0F1 ATP synthase subunit C]

Arcobacter butzleri ED1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ABED_1589, BAK71306.1, BAK71306, F0F1 ATP synthase subunit C]

Arcobacter sp. L

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ABLL_2246, BAK74121.1, G2HYB8, F0F1 ATP synthase subunit C]

Arenimonas composti

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. P873_13315, KFN48785.1, WP_026817558.1, F0F1 ATP synthase subunit C]

Arenimonas malthae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N790_08435, KFN46639.1, KFN46639, F0F1 ATP synthase subunit C]

Arenimonas metalli

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N787_10700, KFN46491.1, WP_034212061.1, F0F1 ATP synthase subunit C]

Arenimonas oryziterrae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N789_13545, KFN42376.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Arthrobacter gangotriensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ADIAG_00850, EMQ99747.1, M7MTK7_9MICC, F0F1 ATP synthase subunit C]

Asticcacaulis benevestitus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ABENE_08840, ESQ92259.1, ESQ92259, F0F1 ATP synthase subunit C]

Asticcacaulis sp. AC402

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ABAC402_03805, ESQ76795.1, V4NUA5, F0F1 ATP synthase subunit C]

Asticcacaulis sp. AC460

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ABAC460_04300, ESQ92113.1, V4RLH8_9CAUL, F0F1 ATP synthase subunit C]

Asticcacaulis sp. AC466

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AEAC466_14035, ESQ83364.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Babela massiliensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BABL1_gene_52, CDK30918.1, BABL1_52, F0F1 ATP synthase subunit C]

Bacillus atrophaeus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BATR1942_16390, ADP34197.1, A0A0H3E4M0, F0F1 ATP synthase subunit C]

Bacillus bataviensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BABA_15812, EKN66590.1, K6C653, F0F1 ATP synthase subunit C]

Bacillus firmus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PBF_05138, EWG12151.1, EWG12151, F0F1 ATP synthase subunit C]

Bacillus macauensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A374_18394, EIT83825.1, I8UA51_9BACI, F0F1 ATP synthase subunit C]

Bacillus methanolicus PB1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PB1_08132, EIJ80314.1, WP_003351756.1, F0F1 ATP synthase subunit C]

Bacillus sonorensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BSONL12_17304, EME73499.1, 452973677, F0F1 ATP synthase subunit C]

Bacillus sp. 1NLA3E

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B1NLA3E_21465, AGK56031.1, 484579233, F0F1 ATP synthase subunit C]

Bacillus vireti

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BAVI_06919, ETI69544.1, W1SNG4, F0F1 ATP synthase subunit C]

Bacillus xiamenensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BA1_01445, EKF37274.1, 31670012, F0F1 ATP synthase subunit C]

Bartonella australis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BAnh1_03400, AGF74223.1, GI:451899760, F0F1 ATP synthase subunit C]

Bartonella bovis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BBbe_03520, ENN92047.1, WP_010700914.1, F0F1 ATP synthase subunit C]

Bartonella henselae

ATPE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BH04120, atpE, CAF27221.1, F0F1 ATP synthase subunit C]

Bartonella schoenbuchensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. m07a_03060, ENN91430.1, WP_007477984.1, F0F1 ATP synthase subunit C]

Bartonella vinsonii berkhoffii

atpE - annotation not available [a.k.a. BVwin_03100, AGF75453.1, GI:451900991, F0F1 ATP synthase subunit C]

Betaproteobacteria bacterium MOLA814

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MOLA814_02712, ESS13698.1, V4YFG1_9PROT, F0F1 ATP synthase subunit C]

Bifidobacterium bombi

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BBOMB_0896, KFF31522.1, KFF31522, F0F1 ATP synthase subunit C]

Bordetella avium

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BAV3219, YP_787714.1, InterPro:IPR000454, F0F1 ATP synthase subunit C]

Bordetella bronchiseptica

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BB4610, NP_891142.1, A0A0H3LSX9, F0F1 ATP synthase subunit C]

Bordetella trematum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAMEA3906487_00936, JPQP01000003_gene1504, 32054238, F0F1 ATP synthase subunit C]

Bradyrhizobium sp. S23321

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. S23_08070, atpC, BAL74027.1, F0F1 ATP synthase subunit C]

Brevibacillus panacihumi

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. T458_05720, EST55305.1, V6MBP8, F0F1 ATP synthase subunit C]

Buchnera aphidicola Ak

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BAKON_003, AEO08376.1, WP_014499178.1, F0F1 ATP synthase subunit C]

Buchnera aphidicola Ua

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BUAMB_003, AEO07838.1, GI:345538971, F0F1 ATP synthase subunit C]

Burkholderia gladioli

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. bgla_1g00870, AEA58790.1, F2LH63, F0F1 ATP synthase subunit C]

Burkholderia glumae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. bglu_1g00720, ACR27275.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Burkholderia pseudomallei K96243

BPSS1948 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, CAH39426.1, GI:52213383, F0F1 ATP synthase subunit C]

Burkholderia sp. YI23

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BYI23_A026550, AET90493.1, G8MAJ7_9BURK, F0F1 ATP synthase subunit C]

Carnobacterium sp. 174

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CAR_c17010, AEB30359.1, F4BM25, F0F1 ATP synthase subunit C]

Carnobacterium sp. WN1359

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Q783_07790, AGY82094.1, caw:Q783_07790, F0F1 ATP synthase subunit C]

Catenovulum agarivorans DS2

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. DS2_13504, EWH09287.1, EWH09287, F0F1 ATP synthase subunit C]

Celeribacter baekdonensis

B30_06386 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EKE72587.1, GI:407202597, F0F1 ATP synthase subunit C]

Celeribacter baekdonensis

B30_11215 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EKE71330.1, EKE71330, F0F1 ATP synthase subunit C]

Cellvibrio mixtus

ALBT01000031_gene1862 - annotation not available [a.k.a. CBP51_11285, ALBT01000031_gene1862, F0F1 ATP synthase subunit C]

Citreicella sp. 357

C357_15636 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EIE50186.1, GI:384465648, F0F1 ATP synthase subunit C]

Citreicella sp. 357

C357_21152 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EIE49000.1, 384464423, F0F1 ATP synthase subunit C]

Clostridium intestinale

ERK32154.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, CINTURNW_0417, U2Q7M0, F0F1 ATP synthase subunit C]

Clostridium tetanomorphum

KAJ53260.1 - annotation not available [a.k.a. CTM_03179, 618854062, F0F1 ATP synthase subunit C]

Clostridium tetanomorphum

CTM_03179 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, CTM_26682, KAJ48774.1, F0F1 ATP synthase subunit C]

Corynebacterium argentoratense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CARG_06420, AGU15408.1, GI:533216080, F0F1 ATP synthase subunit C]

Corynebacterium callunae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H924_05605, AGG66565.1, 459384274, F0F1 ATP synthase subunit C]

Corynebacterium casei

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CCASEI_08640, AHI20291.1, W5XTJ8, F0F1 ATP synthase subunit C]

Corynebacterium diphtheriae

atpE - annotation not available [a.k.a. FRC0043_01449, AEX69675.1, CDPW8_1020, F0F1 ATP synthase subunit C]

Corynebacterium falsenii

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CFAL_07395, AHI03459.1, AHI03459, F0F1 ATP synthase subunit C]

Corynebacterium halotolerans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A605_06140, AGF72234.1, AGF72234, F0F1 ATP synthase subunit C]

Corynebacterium maris

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B841_05755, AGS34624.1, S5STY9_9CORY, F0F1 ATP synthase subunit C]

Corynebacterium resistens

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CRES_1419, AEI09774.1, F8DZ88_CORRG, F0F1 ATP synthase subunit C]

Corynebacterium terpenotabidum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A606_07400, AGP31127.1, WP_020441488.1, F0F1 ATP synthase subunit C]

Corynebacterium vitaeruminis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B843_05835, AHI22552.1, 582019209, F0F1 ATP synthase subunit C]

Cyanothece sp. CCY0110

EAZ93682.1 - annotation not available [a.k.a. CY0110_17842, EAZ93682, F0F1 ATP synthase subunit C]

Defluviimonas sp. 20V17

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. U879_19860, KDB01897.1, WP_035846455.1, F0F1 ATP synthase subunit C]

Desulfitobacterium metallireducens

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. DESME_15480, AHF08273.1, dmt:DESME_15480, F0F1 ATP synthase subunit C]

Ectothiorhodospira sp. PHS1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ECTPHS_08803, EHQ52777.1, 373942232, F0F1 ATP synthase subunit C]

Enterobacter aerogenes

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. EAE_07190, AEG96362.1, YP_004591641, F0F1 ATP synthase subunit C]

Enterobacter cloacae ATCC13047

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ECL_05144, ADF64666.1, A0A0H3CRR9, F0F1 ATP synthase subunit C]

Enterobacter sp. R4368

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H650_15170, AGN86428.1, WP_007369368.1, F0F1 ATP synthase subunit C]

Escherichia albertii KF1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. EAKF1_ch2196, AHE60068.1, W0AR69, F0F1 ATP synthase subunit C]

Exiguobacterium pavilionensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. M467_09805, ERG67572.1, U1LYY6, F0F1 ATP synthase subunit C]

Exiguobacterium sp. MH3

AHA30833.1 - Derived by automated computational analysis using gene prediction method: Protein Homology [a.k.a. U719_14630, exm:U719_14630, 557718908, F0F1 ATP synthase subunit C]

Fulvimarina pelagi

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. FP2506_10131, EAU43194.1, WP_007067168.1, F0F1 ATP synthase subunit C]

Fusobacterium hwasookii

B437_07682 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EJU07539.1, 402257063, F0F1 ATP synthase subunit C]

Gallaecimonas xiamenensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B3C1_05827, EKE75954.1, K2JZX4_9GAMM, F0F1 ATP synthase subunit C]

Gallibacterium anatis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. UMN179_01201, AEC17224.1, gan:UMN179_01201, F0F1 ATP synthase subunit C]

Gammaproteobacteria bacterium BDW918

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. DOK_18055, EIF41409.1, GI:385277427, F0F1 ATP synthase subunit C]

Geobacillus sp. JF8

AGT33726.1 - Derived by automated computational analysis using gene prediction method: GeneMarkS+ [a.k.a. M493_17590, GI:530459150, 530459150, F0F1 ATP synthase subunit C]

Geobacillus stearothermophilus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H839_17448, EZP75308.1, EZP75308, F0F1 ATP synthase subunit C]

Glaciecola nitratireducens

GNIT_3362 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AEP31456.1, GI:347948106, F0F1 ATP synthase subunit C]

Glaciecola psychrophila

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C427_5619, AGH47713.1, AGH47713, F0F1 ATP synthase subunit C]

Gloeobacter kilaueensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GKIL_2235, atpH, AGY58481.1, F0F1 ATP synthase subunit C]

Gordonia neofelifaecis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SCNU_04057, EGD56696.1, GI:326199515, F0F1 ATP synthase subunit C]

Gracilibacillus halophilus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. J416_02636, ENH97972.1, N4WPC4_9BACI, F0F1 ATP synthase subunit C]

Halobacillus halophilus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HBHAL_4601, CCG46939.1, GI:384075444, F0F1 ATP synthase subunit C]

Halobacillus sp. BAB2008

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. D479_00425, ELK49049.1, WP_008632354.1, F0F1 ATP synthase subunit C]

Halomonas anticariensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. L861_13155, EPC00733.1, WP_016418323.1, F0F1 ATP synthase subunit C]

Halomonas elongata

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HELO_4449, CBV44333.1, InterPro:IPR000454, F0F1 ATP synthase subunit C]

Halomonas sp. BJGMMB45

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BJB45_20455, ERL50969.1, GI:545313765, F0F1 ATP synthase subunit C]

Halomonas sp. GFAJ1

MOY_07057 - COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. EHK61099.1, GI:359296858, H0J1A3_9GAMM, F0F1 ATP synthase subunit C]

Halomonas sp. PBN3

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Q671_08735, ERS86508.1, WP_023006402.1, F0F1 ATP synthase subunit C]

Halomonas sp. TD01

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GME_10371, EGP19694.1, 338764736, F0F1 ATP synthase subunit C]

Halyomorpha halys

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HHS_00460, BAO00016.1, BAO00016, F0F1 ATP synthase subunit C]

Helicobacter cetorum MIT007128

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HCW_03245, AFI03930.1, I0ELW1_HELC0, F0F1 ATP synthase subunit C]

Helicobacter cetorum MIT995656

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HCD_02940, AFI05604.1, I0ERN5, F0F1 ATP synthase subunit C]

Helicobacter cinaedi CCUG18818

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HCBAA847_0344, EFR47292.1, HCCG_01840, F0F1 ATP synthase subunit C]

Helicobacter cinaedi PAGU611

atpE - annotation not available [a.k.a. BAM11641.1, HCN_0330, hcp:HCN_0330, F0F1 ATP synthase subunit C]

Helicobacter pylori 26695

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HP_1212, AFV42429.1, C694_06270, F0F1 ATP synthase subunit C]

Helicobacter pylori SouthAfrica7

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HPSA_05950, ADU85158.1, ADU85158, F0F1 ATP synthase subunit C]

Helicobacter suis

EFX43229.1 - Similar to ATP synthase C chain - Helicobacter pylori (Campylobacter pylori) [a.k.a. HSUHS1_0485, GI:321148755, F0F1 ATP synthase subunit C]

Herbaspirillum frisingense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HFRIS_001020, EOA06850.1, 29393703, F0F1 ATP synthase subunit C]

Hylemonella gracilis ATCC19624

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HGR_03857, EGI77922.1, F3KQP8_9BURK, F0F1 ATP synthase subunit C]

Hyphomonas adhaerens

HAD_11040 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KCZ86217.1, A0A069E830_9RHOB, F0F1 ATP synthase subunit C]

Hyphomonas jannaschiana

HJA_05947 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KCZ89770.1, WP_035579453.1, F0F1 ATP synthase subunit C]

Hyphomonas sp. 22II122F38

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HY36_10360, KCZ58254.1, A0A059DXX7, F0F1 ATP synthase subunit C]

Hyphomonas sp. 25B141

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HY29_11690, KCZ55571.1, GI:630773923, F0F1 ATP synthase subunit C]

Hyphomonas sp. BHBN044

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HY30_13685, KCZ59652.1, A0A062UR80_9RHOB, F0F1 ATP synthase subunit C]

Hyphomonas sp. CY54118

HY17_11040 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KCZ45857.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Hyphomonas sp. CY54118

HY17_18410 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KCZ47954.1, KCZ47954, F0F1 ATP synthase subunit C]

Hyphomonas sp. L53140

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. L53_03310, KCZ66366.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Hyphomonas sp. T16B2

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HY2_16305, KCZ47989.1, A0A062TW24, F0F1 ATP synthase subunit C]

Kinetoplastibacterium blastocrithidii

atpE - F0F1 ATP synthase subunit C; Identified by sequence similarity; putative [a.k.a. AFZ83405.1, CKBE_00216, 429338983, F0F1 ATP synthase subunit C]

Labrenzia aggregata

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SIAM614_06448, EAV43402.1, 118436762, F0F1 ATP synthase subunit C]

Lactobacillus acidophilus 30SC

ADZ06933.1 - COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. LAC30SC_03820, ADZ06933, lai:LAC30SC_03820, F0F1 ATP synthase subunit C]

Lactobacillus casei BL23

atpE - annotation not available [a.k.a. CPZ11_00520, LCABL_13830, CAQ66464.1, F0F1 ATP synthase subunit C]

Lactobacillus fabifermentans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. LFAB_10700, ETY73764.1, ETY73764, F0F1 ATP synthase subunit C]

Lactobacillus kefiranofaciens

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B8W86_03310, SAMN02983011_00542, AEG40599.1, F0F1 ATP synthase subunit C]

Lactobacillus ruminis ATCC27782

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. LRC_13630, AEN78615.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Legionella pneumophila Philadelphia

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. lpg2987, AAU29032.1, GI:52630291, F0F1 ATP synthase subunit C]

Leptolyngbya sp. Heron

N836_02705 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, atpH, ESA37439.1, f0f1 atp synthase subunit c, F0f1 atp synthase subunit c, ...]

Leptolyngbya sp. Heron

N836_23710 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, atpH, ESA33073.1, f0f1 atp synthase subunit c, F0f1 atp synthase subunit c, ...]

Listeria innocua

lin2678 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, NP_472007.1, Q927V9_LISIN, F0F1 ATP synthase subunit C]

Listeria weihenstephanensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PWEIH_03921, EUJ40382.1, 577779653, F0F1 ATP synthase subunit C]

Lysinibacillus fusiformis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BFZC1_18315, EFI67158.1, D7WWW9_9BACI, F0F1 ATP synthase subunit C]

Lysinibacillus sphaericus OT4b31

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H131_05154, EON74024.1, 496194783, F0F1 ATP synthase subunit C]

Lysinibacillus varians

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. T479_02810, AHN20509.1, X2GT95_9BACI, F0F1 ATP synthase subunit C]

Marichromatium purpuratum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MARPU_00595, AHF02521.1, WP_005222005.1, F0F1 ATP synthase subunit C]

Marinobacter lipolyticus SM19

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MARLIPOL_10356, EON92016.1, WP_012138088.1, F0F1 ATP synthase subunit C]

Marinobacter nanhaiticus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. J057_08336, ENO15344.1, 478770796, F0F1 ATP synthase subunit C]

Marinobacter santoriniensis

EMP56521.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, MSNKSG1_04281, 469613388, F0F1 ATP synthase subunit C]

Marinobacter santoriniensis

EMP54532.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MSNKSG1_14522, atpE, M7DA51, F0F1 ATP synthase subunit C]

Marinobacter sp. ELB17

EAZ98500.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, MELB17_00165, GI:126627872, F0F1 ATP synthase subunit C]

Marinobacter sp. ES1

Q666_14885 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ERP89170.1, U7FT10_9ALTE, F0F1 ATP synthase subunit C]

Marinobacter sp. ES1

Q666_16695 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ERP85481.1, U7FMF4_9ALTE, F0F1 ATP synthase subunit C]

Marinomonas sp. D104

D104_10955 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ETI59753.1, 566040347, F0F1 ATP synthase subunit C]

Marinomonas sp. D104

D104_14555 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ETI58795.1, W1RQD0_9GAMM, F0F1 ATP synthase subunit C]

Marinomonas ushuaiensis

MUS1_00670 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ETX12155.1, X7E8G8, F0F1 ATP synthase subunit C]

Marinomonas ushuaiensis

MUS1_07800 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ETX11836.1, GI:575466116, F0F1 ATP synthase subunit C]

Meiothermus taiwanensis

AXWR01000007_gene408 - annotation not available [a.k.a. A3962_01945, AXWR01000007_gene408, A0A166L919, F0F1 ATP synthase subunit C]

Melioribacter roseus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MROS_0275, AFN73519.1, I6ZNE4, F0F1 ATP synthase subunit C]

Mesorhizobium amorphae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MEA186_34049, EHH02858.1, 32098644, F0F1 ATP synthase subunit C]

Mesorhizobium sp. L2C084A000

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. X734_01000, ESZ29887.1, GI:563207061, F0F1 ATP synthase subunit C]

Mesorhizobium sp. LNJC398B00

ESY12000.1 - Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit C is part of the membrane proton channel F0; Derived by automated computational analysis using gene prediction method: Protein Homology [a.k.a. X752_11530, GI:563087338, F0F1 ATP synthase subunit C]

Methylophaga lonarensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MPL1_12196, EMR12087.1, WP_009727388.1, F0F1 ATP synthase subunit C]

Moraxella bovoculi

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MBO_06541, KDN24886.1, mbl:AAX09_01545, F0F1 ATP synthase subunit C]

Moraxella catarrhalis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AO384_0896, EA1_01892, EGE27599.1, F0F1 ATP synthase subunit C]

Moraxella macacae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MOMA_04030, ELA09542.1, ELA09542, F0F1 ATP synthase subunit C]

Mycobacterium colombiense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MCOL_V217643, EJO87815.1, J4SFA0_9MYCO, F0F1 ATP synthase subunit C]

Mycobacterium kansasii ATCC12478

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MKAN_06360, AGZ49939.1, mkn:MKAN_06360, F0F1 ATP synthase subunit C]

Mycobacterium mageritense

CDO20181.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, BN978_00633, CDO20181, F0F1 ATP synthase subunit C]

Mycobacterium mageritense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BN978_06759, CDO26205.1, X5KYK1_9MYCO, F0F1 ATP synthase subunit C]

Mycobacterium phlei

atpE - COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. EID14406.1, MPHLEI_11095, AMO62708, F0F1 ATP synthase subunit C]

Mycobacterium thermoresistibile

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. KEK_10072, EHI13517.1, 356480384, F0F1 ATP synthase subunit C]

Mycobacterium vaccae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MVAC_07002, EJZ11187.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Mycoplasma bovoculi

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MYB_00395, AHH45090.1, mbc:MYB_00395, F0F1 ATP synthase subunit C]

Mycoplasma californicum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MCFN_02300, AIA29597.1, WP_038561915.1, F0F1 ATP synthase subunit C]

Mycoplasma gallisepticum S6

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GCW_01720, AHB99592.1, 564749753, F0F1 ATP synthase subunit C]

Mycoplasma girerdii

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MGM1_4320, AIV03798.1, 701169349, F0F1 ATP synthase subunit C]

Nitratireductor indicus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. NA8A_16086, EKF41387.1, GI:407428706, F0F1 ATP synthase subunit C]

Nitratireductor pacificus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. NA2_06278, EKF19926.1, 407300803, F0F1 ATP synthase subunit C]

Nocardia brasiliensis

O3I_006245 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AFT99211.1, AFT99211, F0F1 ATP synthase subunit C]

Nocardia brasiliensis

O3I_032895 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AFU04528.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Nocardia brasiliensis

O3I_033550 - COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. AFU04659.1, K0F4W5_9NOCA, 407310758, F0F1 ATP synthase subunit C]

Novosphingobium lindaniclasticum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. L284_07200, EQB17615.1, WP_007013775.1, F0F1 ATP synthase subunit C]

Novosphingobium nitrogenifigens

Y88_0535 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EGD58479.1, F1ZAB3_9SPHN, F0F1 ATP synthase subunit C]

Novosphingobium resinovorum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BV97_01090, BES08_07485, EZP83898.1, F0F1 ATP synthase subunit C]

Oceanibulbus indolifex

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. OIHEL45_04160, EDQ05976.1, 161381567, F0F1 ATP synthase subunit C]

Oceanimonas sp. GK1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GU3_02230, AEY00203.1, WP_014290939.1, F0F1 ATP synthase subunit C]

Oxalobacter formigenes OXCC13

atpE - annotation not available [a.k.a. BRW84_00925, OFBG_01828, ARQ45028, F0F1 ATP synthase subunit C]

Paenibacillus alvei

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PAALTS15_07199, EPY08012.1, WP_021258908.1, F0F1 ATP synthase subunit C]

Paenibacillus polymyxa M1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A7312_00700, EL23_09615, AOU00_10385, F0F1 ATP synthase subunit C]

Paenibacillus sabinae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PSAB_22510, AHV99389.1, X5A6H0, F0F1 ATP synthase subunit C]

Paenibacillus terrae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HPL003_04780, AET57723.1, GI:357199826, F0F1 ATP synthase subunit C]

Pandoraea sp. SD62

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C266_20175, EON11914.1, R7WXH1_9BURK, F0F1 ATP synthase subunit C]

Pantoea agglomerans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CRM79_14350, AL522_04435, BW31_01345, F0F1 ATP synthase subunit C]

Pantoea sp. Sc1

S7A_04070 - COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. EIB97661.1, EIB97661, 380736598, F0F1 ATP synthase subunit C]

Planococcus antarcticus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BBH88_06940, EIM07360.1, A1A1_06142, F0F1 ATP synthase subunit C]

Planococcus donghaensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GPDM_16151, EGA88247.1, pdg:BCM40_03215, F0F1 ATP synthase subunit C]

Planococcus sp. PAMC21323

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Plano_2397, AIY06362.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Planomicrobium glaciei

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAMN04487975_10986, ETP67753.1, G159_15895, F0F1 ATP synthase subunit C]

Plautia stali

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. E05_29000, BAN97666.1, GI:549070704, F0F1 ATP synthase subunit C]

Pontibacillus halophilus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N781_01460, KGX93889.1, KGX93889, F0F1 ATP synthase subunit C]

Pontibacillus litoralis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N784_04635, KGX86444.1, 717927085, F0F1 ATP synthase subunit C]

Pontibacillus marinus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N783_10125, KGX87281.1, GI:717927952, F0F1 ATP synthase subunit C]

Profftella armatura

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SSDC_01080, AGS06905.1, GI:527122380, F0F1 ATP synthase subunit C]

Providencia burhodogranariea

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. OOA_18699, EKT53373.1, K8VYQ7, F0F1 ATP synthase subunit C]

Providencia rettgeri Dmel1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. OOC_01762, EKT59678.1, WP_004093904.1, F0F1 ATP synthase subunit C]

Pseudogulbenkiania sp. NH8B

NH8B_2468 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, BAK77282.1, G2J5D7, F0F1 ATP synthase subunit C]

Pseudomonas aeruginosa

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CAZ10_15085, PAMH19_6429, CAZ03_15110, F0F1 ATP synthase subunit C]

Pseudomonas alkylphenolia

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PSAKL28_52730, AIL64413.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas denitrificans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H681_25300, AGI26927.1, 472252213, F0F1 ATP synthase subunit C]

Pseudomonas fluorescens HK44

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. HK44_012910, EXF91707.1, 589145505, F0F1 ATP synthase subunit C]

Pseudomonas fluorescens NCIMB11764

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B723_05205, B723_32360, ERP44243.1, F0F1 ATP synthase subunit C]

Pseudomonas mandelii PD30

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. V466_21555, KDD66887.1, GI:633677302, F0F1 ATP synthase subunit C]

Pseudomonas mendocina EGDAQ5

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. O203_00835, ERH52455.1, 5106922, F0F1 ATP synthase subunit C]

Pseudomonas mendocina NK01

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MDS_4947, AEB60978.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas moraviensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PMO01_27855, ETF05447.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas poae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAMN04490208_3232, CDH05_03985, H045_20975, F0F1 ATP synthase subunit C]

Pseudomonas psychrotolerans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SB14R_05200, SAMN05216279_102165, PPL19_08791, F0F1 ATP synthase subunit C]

Pseudomonas putida CSV86

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CSV86_19083, EKX83610.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas putida S16

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PPS_5278, AEJ15805.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas sp. 20BN

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BN1079_02600, CDZ95267.1, A0A078LY74_9PSED, F0F1 ATP synthase subunit C]

Pseudomonas sp. CF149

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. CF149_21218, EPJ91592.1, S6J1N8, F0F1 ATP synthase subunit C]

Pseudomonas sp. Chol1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C211_13751, EKM95380.1, 32112027, F0F1 ATP synthase subunit C]

Pseudomonas sp. Lz4W

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B195_01070, EMI09153.1, GI:459963182, F0F1 ATP synthase subunit C]

Pseudomonas sp. M1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PM1_0229060, ETM64571.1, 568071708, F0F1 ATP synthase subunit C]

Pseudomonas sp. M47T1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PMM47T1_06886, EIK97490.1, I4N7Q0, F0F1 ATP synthase subunit C]

Pseudomonas sp. RIT357

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. BW43_01157, EZP68267.1, GI:612110110, F0F1 ATP synthase subunit C]

Pseudomonas sp. TKP

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. U771_31952, AHC38856.1, V9R7R4, F0F1 ATP synthase subunit C]

Pseudomonas sp. VLB120

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PVLB_25680, AGZ37913.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri ATCC14405

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PstZobell_17137, EHY79148.1, WP_003284846.1, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri CCUG 29243

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A458_21745, AFM35558.1, GI:390985565, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri DSM10701

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PS273GM_07420, AFN79888.1, PSJM300_19185, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri KOS6

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B597_004870, EWC42319.1, A0A061JVB5, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri MF28

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. L686_21060, EQM74194.1, WP_003097235.1, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri NF13

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B381_20621, EMD98148.1, M2VEM6, F0F1 ATP synthase subunit C]

Pseudomonas stutzeri TS44

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. YO5_14785, EIK51610.1, EIK51610, F0F1 ATP synthase subunit C]

Pseudomonas syringae CC1557

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N018_25805, AHG43461.1, psyr:N018_25805, F0F1 ATP synthase subunit C]

Pseudomonas syringae maculicola

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PMA4326_23376, EGH61751.1, F3HQY1, F0F1 ATP synthase subunit C]

Pseudomonas syringae tomato

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PSPTO5604, PSPTO_5604, AAO59017.1, F0F1 ATP synthase subunit C]

Psychromonas sp. CNPT3

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PCNPT3_00185, AGH79979.1, M4U157_9GAMM, F0F1 ATP synthase subunit C]

Rahnella aquatilis HX2

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Q7S_22410, AFE60687.1, WP_004093904.1, F0F1 ATP synthase subunit C]

Ralstonia pickettii DTP0602

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. N234_20350, AGW92383.1, rpj:N234_20350, F0F1 ATP synthase subunit C]

Ralstonia sp. AU1208

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C404_24350, EPX95518.1, S9RTF3, F0F1 ATP synthase subunit C]

Raoultella ornithinolytica

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAMEA3181514_05356, CAC00_05140, TE10_02345, F0F1 ATP synthase subunit C]

Rhizobium grahamii

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RGCCGE502_04290, EPE99373.1, S3IKP3, F0F1 ATP synthase subunit C]

Rhizobium leguminosarum CB782

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A4U53_27595, BMW22_17065, BA011_24415, F0F1 ATP synthase subunit C]

Rhizobium sp. CCGE510

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RCCGE510_20299, EJT03345.1, EJT03345, F0F1 ATP synthase subunit C]

Rhizobium sp. LPU83

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. LPU83_0974, CDM56650.1, WP_016552934.1, F0F1 ATP synthase subunit C]

Rhodanobacter fulvus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. UU9_13658, EIL88166.1, GI:388431062, F0F1 ATP synthase subunit C]

Rhodanobacter spathiphylli

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. UU7_07646, EIL93699.1, WP_007807016.1, F0F1 ATP synthase subunit C]

Rhodanobacter thiooxydans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RHOFW104T7_15860, UUA_12423, EIL98271.1, F0F1 ATP synthase subunit C]

Rhodobacteraceae bacterium HTCC2150

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RB2150_13971, EBA05202.1, WP_008183067.1, F0F1 ATP synthase subunit C]

Rhodobacterales bacterium HTCC2255

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. OM2255_10361, EAU52552.1, EAU52552, F0F1 ATP synthase subunit C]

Rhodococcus pyridinivorans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Y013_24595, AHD23537.1, GI:568236632, F0F1 ATP synthase subunit C]

Rhodococcus rhodnii

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Rrhod_3813, EOM74935.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Rhodococcus triatomae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. G419_11737, EME20335.1, 452762037, F0F1 ATP synthase subunit C]

Rhodonellum psychrophilum

P872_18910 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ERM82255.1, GI:548769709, F0F1 ATP synthase subunit C]

Rickettsia akari

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A1C_00255, ABV74384.1, GI:157799130, F0F1 ATP synthase subunit C]

Rickettsia australis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MC5_00255, AFC70488.1, H8K8W8, F0F1 ATP synthase subunit C]

Rickettsia bellii OSU85389

A1I_00410 - COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. ABV78488.1, ABV78488, F0F1 ATP synthase subunit C]

Rickettsia canadensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A1E_00095, ABV72972.1, A8EX89, F0F1 ATP synthase subunit C]

Rickettsiales bacterium Ac37b

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. NOVO_02920, AIL64975.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Roseivivax halodurans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. OCH239_16300, ETX15386.1, GI:575469732, F0F1 ATP synthase subunit C]

Roseivivax isoporae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RISW2_20210, ETX29975.1, X7FB18_9RHOB, F0F1 ATP synthase subunit C]

Roseivivax sp. 22IIs10s

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ATO8_20699, ETW10738.1, W4HE99, F0F1 ATP synthase subunit C]

Roseobacter sp. AzwK3b

EDM70578.1 - F0F1 ATP synthase subunit C; COG1266 Predicted metal-dependent membrane protease [a.k.a. RAZWK3B_05517, 149810737, F0F1 ATP synthase subunit C]

Roseobacter sp. SK20926

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RSK20926_05882, EBA17241.1, A4ES71, F0F1 ATP synthase subunit C]

Roseovarius sp. TM1035

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RTM1035_17152, EDM33733.1, A6DWF9, F0F1 ATP synthase subunit C]

Ruminococcus flavefaciens 007c

EWM52893.1 - Produces ATP from ADP in the presence of a proton gradient across the membrane; subunit C is part of the membrane proton channel F0; Derived by automated computational analysis using gene prediction method: GeneMarkS+ [a.k.a. RF007C_14870, F0F1 ATP synthase subunit C, GI:585218481]

Ruminococcus flavefaciens 007c

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RF007C_14870, RF007C_14875, EWM52894.1, F0F1 ATP synthase subunit C]

Sagittula stellata

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SSE37_15536, EBA06308.1, A3K9D6, F0F1 ATP synthase subunit C]

Salimicrobium sp. MJ3

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. MJ3_08581, EKE31416.1, WP_008590466.1, F0F1 ATP synthase subunit C]

Serratia fonticola RB25

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Z042_11850, AHG20243.1, WP_004093904.1, F0F1 ATP synthase subunit C]

Serratia sp. M24T3

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SPM24T3_14541, EIC83936.1, EIC83936, F0F1 ATP synthase subunit C]

Simiduia agarivorans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. M5M_12515, AFU99659.1, K4KKK6, F0F1 ATP synthase subunit C]

Sinorhizobium americanum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAMCCGM7_Ch0873, SAMCCGM7_c0901, KEC81516.1, F0F1 ATP synthase subunit C]

Sinorhizobium meliloti

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SMc00870, CAC45408.1, 1232477, F0F1 ATP synthase subunit C]

Sphaerotilus natans

X805_27750 - annotation not available [a.k.a. KDB51624.1, GI:633286688, F0F1 ATP synthase subunit C]

Sphingobium baderi

L485_12275 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EQB00717.1, 530257967, F0F1 ATP synthase subunit C]

Sphingobium baderi

L485_18875 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EQA98140.1, GI:530255335, F0F1 ATP synthase subunit C]

Sphingobium chlorophenolicum

BV95_00951 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KEQ54722.1, KEQ54722, F0F1 ATP synthase subunit C]

Sphingobium herbicidovorans

KFG91496.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, BV98_000693, WP_017501321.1, F0F1 ATP synthase subunit C]

Sphingobium herbicidovorans

KFG89630.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, BV98_002437, InterPro:IPR000454, F0F1 ATP synthase subunit C]

Sphingobium lactosutens

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RLDS_05190, EQB17352.1, T0HWB2_9SPHN, F0F1 ATP synthase subunit C]

Sphingobium sp. C100

C100_01875 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ETI65508.1, W1SEF9, F0F1 ATP synthase subunit C]

Sphingobium sp. C100

C100_08740 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, ETI64161.1, W1S402, F0F1 ATP synthase subunit C]

Sphingobium ummariense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. M529_09180, EQB32408.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Sphingobium yanoikuyae

CP98_04167 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AX777_17040, KEZ16477.1, F0F1 ATP synthase subunit C]

Sphingomonas paucimobilis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A8O16_13920, BV96_02603, EZP71329.1, F0F1 ATP synthase subunit C]

Sphingomonas sanxanigenens

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. NX02_00315, AHE51832.1, W0A5S7_9SPHN, F0F1 ATP synthase subunit C]

Spiribacter salinus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SPISAL_08400, AGM41774.1, WP_016354081.1, F0F1 ATP synthase subunit C]

Spiribacter sp. UAHSP71

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SPICUR_09515, AGY92822.1, U5T971, F0F1 ATP synthase subunit C]

Spiroplasma apis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAPIS_v1c00490, AHB35896.1, V5RIG0_SPIAP, F0F1 ATP synthase subunit C]

Spiroplasma chrysopicola

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SCHRY_v1c00850, AGM24672.1, 506965968, F0F1 ATP synthase subunit C]

Spiroplasma culicicola

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SCULI_v1c00560, AHI52397.1, 583840477, F0F1 ATP synthase subunit C]

Spiroplasma diminutum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SDIMI_v3c00510, AGR41755.1, GI:525041511, F0F1 ATP synthase subunit C]

Spiroplasma melliferum

atpE - annotation not available [a.k.a. ELL44513.1, SMIPMB4A_v3c5930, 434155571, F0F1 ATP synthase subunit C]

Spiroplasma sabaudiense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SSABA_v1c00490, AHI53461.1, 583839542, F0F1 ATP synthase subunit C]

Spiroplasma syrphidicola

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SSYRP_v1c01050, AGM25701.1, AGM25701, F0F1 ATP synthase subunit C]

Spiroplasma taiwanense

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. STAIW_v1c00540, AGR40749.1, stai:STAIW_v1c00540, F0F1 ATP synthase subunit C]

Sporocytophaga myxococcoides

MYP_2968 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, GAL85739.1, A0A098LH30, F0F1 ATP synthase subunit C]

Sporolactobacillus laevolacticus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. P343_07105, EST12393.1, V6IY62, F0F1 ATP synthase subunit C]

Staphylococcus agnetis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B9M88_08280, SAGN_09982, KFE40987.1, F0F1 ATP synthase subunit C]

Staphylococcus chromogenes

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SCHR_09859, KDP12159.1, GI:643339357, F0F1 ATP synthase subunit C]

Staphylococcus intermedius

CAIB01000243_gene2174 - annotation not available [a.k.a. B4W74_11555, A0A2A4H283, CAIB01000243_gene2174, F0F1 ATP synthase subunit C]

Staphylococcus massiliensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C273_07987, EKU47164.1, K9AIN6, F0F1 ATP synthase subunit C]

Staphylococcus simulans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SSIM_11670, ERS92528.1, WP_002481788.1, F0F1 ATP synthase subunit C]

Staphylococcus warneri SG1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A284_03925, AGC90106.1, 443425203, F0F1 ATP synthase subunit C]

Stenotrophomonas maltophilia 5BAI2

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. STRNTR1_2784, B7H26_06505, BWP19_11915, F0F1 ATP synthase subunit C]

Streptococcus agalactiae LMG14747

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SAG0136_09985, ESV55508.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Streptococcus agalactiae NEM316

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. gbs0875, NP_735325.1, Q8E5V4, F0F1 ATP synthase subunit C]

Streptococcus anginosus DORA7

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Q615_SPAC00113G0193, ETI85518.1, 566219966, F0F1 ATP synthase subunit C]

Streptococcus canis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SCAZ3_04345, EIQ81619.1, I7MXV1, F0F1 ATP synthase subunit C]

Streptococcus dysgalactiae ATCC27957

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SDD27957_03575, EFY02379.1, E7PVE9_STRDY, F0F1 ATP synthase subunit C]

Streptococcus dysgalactiae equisimilis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SDSE_0764, CCI62261.1, 410439633, F0F1 ATP synthase subunit C]

Streptococcus iniae

AHY15985.1 - F0F1 ATP synthase subunit C; Produces ATP from ADP in the presence of a proton gradient across the membrane; subunit C is part of the membrane proton channel F0; Derived by automated computational analysis using gene prediction method: Protein Homology [a.k.a. BKX95_01635, DQ08_05865, A0A1J0MZR9, F0F1 ATP synthase subunit C]

Streptococcus mutans GS5

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A6J86_03890, AFM81877.1, SMUGS5_06910, F0F1 ATP synthase subunit C]

Streptococcus oligofermentans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. I872_02995, AGK70704.1, N0CCR0_STRCR, F0F1 ATP synthase subunit C]

Streptococcus pseudopneumoniae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SPPN_07420, AEL10910.1, G0IB49, F0F1 ATP synthase subunit C]

Streptococcus pyogenes

atpE - annotation not available [a.k.a. CRD75_02970, HKU360_00585, AIW24411.1, F0F1 ATP synthase subunit C]

Streptococcus ratti

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. D822_03199, EJN94231.1, SRA_06836, F0F1 ATP synthase subunit C]

Streptococcus salivarius 57I

Ssal_01686 - annotation not available [a.k.a. AEJ53943.1, F8HFJ6_STRE5, AEJ53943, F0F1 ATP synthase subunit C]

Streptococcus suis R61

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SSUR61_0313, EHC03759.1, 353534125, F0F1 ATP synthase subunit C]

Streptococcus tigurinus 1366

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B7730_09425, B7728_04815, B7726_05210, F0F1 ATP synthase subunit C]

Streptococcus tigurinus AZ3a

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. H354_09501, EMG31908.1, WP_001054552.1, F0F1 ATP synthase subunit C]

Streptomyces hygroscopicus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SHJG_6449, AEY91716.1, AEY91716, F0F1 ATP synthase subunit C]

Sulfitobacter donghicola

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. DSW25_03505, KEJ90972.1, A0A073IZZ9_9RHOB, F0F1 ATP synthase subunit C]

Sulfuricurvum sp. RIFRC1

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B649_01530, YP_007527315.1, 14762756, F0F1 ATP synthase subunit C]

Sulfurimonas sp. AST10

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. M947_06485, EQB39636.1, T0JNE0, F0F1 ATP synthase subunit C]

Sulfurovum sp. AR

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. SULAR_06188, EIF50935.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Synechococcus sp. KORDI100

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. KR100_13575, atpH, AII44377.1, F0F1 ATP synthase subunit C]

Synechococcus sp. KORDI49

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpH, KR49_06290, AII46059.1, F0F1 ATP synthase subunit C]

Synechococcus sp. KORDI52

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. KR52_05110, atpH, AII48524.1, F0F1 ATP synthase subunit C]

Synechococcus sp. RS9916

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. RS9916_34617, atpH, EAU74749.1, F0F1 ATP synthase subunit C]

Thalassolituus oleivorans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. TOL_3700, CCU74083.1, WP_015488783.1, F0F1 ATP synthase subunit C]

Thalassotalea sp. ND16A

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. ND16A_1025, KGJ96832.1, GI:694344060, F0F1 ATP synthase subunit C]

Thauera linaloolentis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C666_13760, ENO86181.1, N6XWM0_9RHOO, F0F1 ATP synthase subunit C]

Thauera sp. 27

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. B447_05895, ENO81935.1, 479293835, F0F1 ATP synthase subunit C]

Thauera sp. 63

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C664_13859, ENO76637.1, GI:479288537, F0F1 ATP synthase subunit C]

Thauera terpenica

M622_05815 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EPZ14498.1, T0AV67_9RHOO, F0F1 ATP synthase subunit C]

Thauera terpenica

M622_06660 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, EPZ14253.1, WP_021250710.1, F0F1 ATP synthase subunit C]

Thermotoga maritima

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. TM_1615, AHD18489.1, THEMA_06175, F0F1 ATP synthase subunit C]

Thermotoga sp. Mc24

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Mc24_03883, KHC91878.1, WP_004082074.1, F0F1 ATP synthase subunit C]

Thioalkalimicrobium aerophilum

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. THIAE_10235, AHF02088.1, W0DXS8_9GAMM, F0F1 ATP synthase subunit C]

Thioalkalivibrio sulfidiphilus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. Tgr7_3310, ACL74377.1, 219997775, F0F1 ATP synthase subunit C]

Thioalkalivibrio thiocyanoxidans ARh4

AHE99705.1 - Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit C is part of the membrane proton channel F0; Derived by automated computational analysis using gene prediction method: Protein Homology [a.k.a. THITH_16990, 570728397, F0F1 ATP synthase subunit C]

Thioclava pacifica

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. TP2_13410, KEO50880.1, WP_038079616.1, F0F1 ATP synthase subunit C]

Thioclava sp. 13D2W2

DW2_03234 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KFE36289.1, A0A085TZZ2, F0F1 ATP synthase subunit C]

Thioclava sp. 13D2W2

DW2_05645 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KFE36088.1, 34440915, F0F1 ATP synthase subunit C]

Thioclava sp. DT234

DT23_06090 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KEO55539.1, KEO55539, F0F1 ATP synthase subunit C]

Thioclava sp. DT234

DT23_06700 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, KEO53853.1, A0A074JE31, F0F1 ATP synthase subunit C]

Tistrella mobilis

TMO_1654 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, AFK53493.1, I3TL55_TISMK, F0F1 ATP synthase subunit C]

Vibrio brasiliensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. VIBR0546_08204, EGA65868.1, 323312740, F0F1 ATP synthase subunit C]

Vibrio caribbeanicus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. VIBC2010_13346, EFP97606.1, E3BH83_9VIBR, F0F1 ATP synthase subunit C]

Vibrio genomosp.

A1QO_06680 - annotation not available [a.k.a. AJYQ01000119_gene1506, F0F1 ATP synthase subunit C, A0A1E5BFZ4]

Vibrio jasicida

BAOA01000079_gene3047 - annotation not available [a.k.a. B6K85_09690, BAOA01000079_gene3047, A0A2A2N9S8, F0F1 ATP synthase subunit C]

Vibrio scophthalmi

EGU39334.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. VIS19158_05989, atpE, EGU39334, F0F1 ATP synthase subunit C]

Vibrio scophthalmi

EGU33042.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. VIS19158_22132, atpE, 31590863, F0F1 ATP synthase subunit C]

Vibrio sinaloensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. VISI1226_16960, EGA70968.1, GI:323317985, F0F1 ATP synthase subunit C]

Vibrio sp. EJY3

AEX23565.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, VEJY3_15475, GI:369842421, F0F1 ATP synthase subunit C]

Vibrio sp. N418

EGU33326.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, VIBRN418_12831, F9RD39_VIBSN, F0F1 ATP synthase subunit C]

Vibrio sp. N418

EGU30353.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, VIBRN418_19548, EGU30353, F0F1 ATP synthase subunit C]

Vibrio tubiashii

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. IX91_15390, EGU57795.1, VITU9109_19949, F0F1 ATP synthase subunit C]

Vibrio vulnificus

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. VV3256, AIL72046.1, VV93_v1c29780, F0F1 ATP synthase subunit C]

Viridibacillus arenosi

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. C176_03578, ETT87198.1, WP_038180035.1, F0F1 ATP synthase subunit C]

Weissella koreensis

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. WKK_02895, AEJ23453.1, 338854287, F0F1 ATP synthase subunit C]

Weissella oryzae

GAK30029.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, WOSG25_011190, A0A069CRK3_9LACT, F0F1 ATP synthase subunit C]

Weissella oryzae

GAK30030.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. WOSG25_011200, atpE, WP_027698173.1, F0F1 ATP synthase subunit C]

Wolbachia sp. Ooc

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. wOo_00490, CCF77919.1, 398649749, F0F1 ATP synthase subunit C]

Xanthomonas axonopodis phaseoli

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PK68_17985, XppCFBP6546P_16065, NY99_01355, F0F1 ATP synthase subunit C]

Xanthomonas fragariae

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. PD5205_03271, O1K_19291, ENZ93785.1, F0F1 ATP synthase subunit C]

Xanthomonas fuscans

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. XFF4834R_chr35500, NB99_04405, CDF62978.1, F0F1 ATP synthase subunit C]

Xanthomonas translucens

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. A989_02505, ELQ16118.1, ATP synthase subunit c, F0F1 ATP synthase subunit C]

Xylella fastidiosa PLS229

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. AF72_05555, EWS78408.1, 586884054, F0F1 ATP synthase subunit C]

Youngiibacter fragilis

ETA82548.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, T472_0200500, 564136418, F0F1 ATP synthase subunit C]

Youngiibacter fragilis

ETA81197.1 - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. atpE, T472_0207710, GI:564134926, F0F1 ATP synthase subunit C]

actinobacterium acAMD5

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. GM45_6080, KGA08351.1, KGA08351, F0F1 ATP synthase subunit C]

alpha proteobacterium MA2

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. M2A_1538, GAK45039.1, GI:665495252, F0F1 ATP synthase subunit C]

endosymbiont of Acanthamoeba

atpE - ATP synthase subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation [a.k.a. I862_06030, AIF81760.1, GI:665991999, F0F1 ATP synthase subunit C]

Tsukamurella paurometabola

Tpau_2292 - KEGG: msm:MSMEG_4941 F0F1 ATP synthase subunit C; TIGRFAM: ATP synthase F0, C subunit; PFAM: H+transporting two-sector ATPase C subunit [a.k.a. ADG78899.1, D5UQC9, WP_013126921.1]

Bibersteinia trehalosi

AHG85226.1 - F0F1 ATP synthase subunit C PRK06876; ATP synthase subunit c of Gammaproteobacteria UniRef RepID=ATPL_VIBF1 [a.k.a. F543_23720, ATP synthase subunit c, 575453214]

Rhodopirellula baltica

RB4917 - PMID: 9425287 best DB hits: BLAST: gb:AAC38058.1; (AF028006) ATP synthase gamma subunit C-terminus; E=7e-27 gb:AAC38057.1; (AF028006) ATP synthase gamma subunit N-terminus; E=1e-13 swissprot:P00837; ATPG_ECOLI ATP SYNTHASE GAMMA CHAIN -----; E=2e-13 COG: atpG; COG0224 F0F1-type ATP synthase gamma subunit; E=2e-14 PFAM: PF00231; ATP synthase; E=3.3e-07 [a.k.a. atpG, NP_866394.1, WP_007340302.1]

Bacteroides caccae

EDM21998.1 - ATP synthase subunit C; KEGG: bth:BT1295 2.7e-74 V-type sodium ATP synthase subunit K; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score: 9.46 [a.k.a. BACCAC_00370, 31616426, A5ZBX9]

Acidaminococcus fermentans

Acfer_1714 - TIGRFAM: ATP synthase F0, C subunit; PFAM: H+transporting two-sector ATPase C subunit; KEGG: lbu:LBUL_0638 F0F1 ATP synthase subunit C [a.k.a. ADB48070.1, ADB48070, GI:283953267]

Variovorax paradoxus S110

Vapar_0367 - TIGRFAM: ATP synthase F0, C subunit; PFAM: H+transporting two-sector ATPase C subunit; KEGG: mms:mma_3632 F0F1 ATP synthase subunit C [a.k.a. ACS17030.1, C5CYC6, InterPro:IPR000454]

Bacteroides coprocola

EDU99190.1 - ATP synthase subunit C; KEGG: bth:BT1295 3.3e-69 V-type sodium ATP synthase subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score: 9.46 [a.k.a. BACCOP_03940, InterPro:IPR002379, B3JPH9]

Bacteroides intestinalis

EDV06746.1 - ATP synthase subunit C; KEGG: bth:BT1295 5.2e-71 V-type sodium ATP synthase subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score: 9.46 [a.k.a. BACINT_01845, 189437761, GI:189437761]

Bacteroides ovatus

ntpK - ATP synthase subunit C; KEGG: bth:BT1295 3.1e-73 V-type sodium ATP synthase subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score:9.46 [a.k.a. BACOVA_00077, EDO14220.1, 156112475]

Alistipes putredinis

EDS03228.1 - ATP synthase subunit C; KEGG: bfs:BF2743 3.1e-41 putative V(vacuolar)-type Na+-ATP synthase subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score: 9.46 [a.k.a. ALIPUT_02769, GI:167659098, B0N042]

Bacteroides stercoris

EDS13733.1 - ATP synthase subunit C; KEGG: bfs:BF2743 1.1e-70 putative V(vacuolar)-type Na+-ATP synthase subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score: 9.46 [a.k.a. BACSTE_02869, 167697154, GI:167697154]

Bacteroides uniformis

EDO54334.1 - ATP synthase subunit C; KEGG: bfs:BF2743 3.6e-33 putative V(vacuolar)-type Na+-ATP synthase subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score:9.50 [a.k.a. BACUNI_01810, WP_005827396.1, 156860903]

Anaerobaculum mobile

Anamo_1908 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; PFAM: ATP synthase subunit C; Belongs to the V-ATPase proteolipid subunit family [a.k.a. AFM22494.1, amo:Anamo_1908, InterPro:IPR000454]

Caldisphaera lagunensis

Calag_1414 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; PFAM: ATP synthase subunit C; Belongs to the V-ATPase proteolipid subunit family [a.k.a. AFZ71121.1, InterPro:IPR000454, clg:Calag_1414]

Aciduliprofundum sp. MAR08339

AGB05162.1 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; PFAM: ATP synthase subunit C [a.k.a. AciM339_1300, InterPro:IPR000454, acf:AciM339_1300]

Marinitoga piezophila

Marpi_0565 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; PFAM: ATP synthase subunit C [a.k.a. AEX85006.1, InterPro:IPR000454, H2J5M0_MARPK]

Thioflavicoccus mobilis

Thimo_1490 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; PFAM: ATP synthase subunit C [a.k.a. AGA90279.1, 431829166, L0GY92]

Thiorhodovibrio sp. 970

EIC22398.1 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; PFAM: ATP synthase subunit C [a.k.a. Thi970DRAFT_02658, EIC22398, InterPro:IPR000454]

Burkholderia rhizoxinica

RBRH_00825 - ATP synthase alpha chain (EC 3.6.3.14); COG: F0F1-type ATP synthase, alpha subunit; Pfam: ATP synthase alpha/beta family, nucleotide-binding domain::PF00006 ATP synthase alpha/beta chain, C terminal domain::PF00306 [a.k.a. CBW73671.1, 3.6.3.14, GI:312166668]

Anaplasma marginale Florida

atpE - ATP synthase C chain (AtpE); Psort: bacterial inner membrane --- Certainty= 0.505(Affirmative); COG0636 AtpE F0F1-type ATP synthase c subunit/Archaeal/vacuolar-type H+-ATPase subunit K [a.k.a. AMF_841, ACM49671.1, B9KGW7_ANAMF]

Streptococcus anginosus F0211

EFU22857.1 - KEGG: sez:Sez_0792 1.1e-19 atpE; F0F1 ATP synthase subunit C ; K02110 F-type H+-transporting ATPase subunit c; Psort location: Cytoplasmic, score: 7.50 [a.k.a. HMPREF0813_00537, 315189156, sans:DK43_07010]

Natronococcus occultus

Natoc_2448 - F0F1-type ATP synthase, subunit c/archaeal/vacuolar-type H+-ATPase, subunit K; IMG reference gene:2506731164; PFAM: ATP synthase subunit C [a.k.a. AGB38223.1, L0K295_9EURY, WP_015321665.1]

Parabacteroides merdae

EDN86857.1 - ATP synthase subunit C; KEGG: pgi:PG1807 4.1e-48 atpK; v-type ATPase, subunit K K02124; COG: COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Psort location: CytoplasmicMembrane, score:9.46 [a.k.a. PARMER_02221, 154087812, WP_005638767.1]

Coleofasciculus chthonoplastes

EDX75866.1 - ATP synthase ab C terminal domain protein; [C] COG0055 F0F1-type ATP synthase, beta subunit [a.k.a. MC7420_6521, ATP synthase ab C terminal domain protein, EDX75866]

Zymomonas mobilis pomaceae

Zymop_0561 - PFAM: H+transporting two-sector ATPase C subunit; KEGG: pla:Plav_0696 F0F1 ATP synthase subunit C [a.k.a. AEI37463.1, H+transporting two-sector ATPase C subunit, InterPro:IPR000454]

Carnobacterium maltaromaticum

ntpK - V-type sodium ATPase subunit K; [C] COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K; Belongs to the V-ATPase proteolipid subunit family [a.k.a. BN424_1636, CCO11077.2, UniProtKB/TrEMBL:K8E3V0]

Methylomonas methanica

Metme_0837 - ATP synthase subunit beta; SMART: ATPase, AAA+ type, core; TIGRFAM: ATPase, F1 complex, beta subunit; KEGG: mca:MCA1556 F0F1 ATP synthase subunit beta; HAMAP: ATPase, F1 complex, beta subunit; PFAM: ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain; ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal; ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal [a.k.a. AEF99275.1, 3.6.3.14, 333806606]

Bacteroides caccae

EDM20578.1 - TrkA C-terminal domain protein; KEGG: ilo:IL2624 0.066 atpE; F0F1-type ATP synthase, subunit c; COG: COG0475 Kef-type K+ transport systems, membrane components; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. BACCAC_02038, InterPro:IPR006153, bcac:CGC64_09025]

Prevotella stercorea

EHJ41511.1 - Uncharacterized protein; KEGG: reh:H16_A3642 0.0089 atpE; F0F1 ATP synthase subunit C K02110; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. HMPREF0673_00687, EHJ41511, G6AVQ0_9BACT]

Veillonella atypica KON

EKY21157.1 - Uncharacterized protein; KEGG: neu:NE0201 0.0011 atpE; F0F1 ATP synthase subunit C K02110; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. HMPREF0870_00222, L1Q0J9_9FIRM, InterPro:IPR007563]

Leptotrichia sp. F0557

ERK52973.1 - KEGG: nmu:Nmul_A0305 0.0048 F0F1 ATP synthase subunit C; K02110 F-type H+-transporting ATPase subunit c; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. HMPREF1552_00612, U2RHG8, 544240376]

Leptotrichia sp. F0581

ERL04237.1 - Uncharacterized protein; KEGG: nmu:Nmul_A0305 0.0099 F0F1 ATP synthase subunit C; K02110 F-type H+-transporting ATPase subunit c; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. HMPREF9108_02138, GI:544316686, ERL04237]

Prevotella copri

EFB36105.1 - KEGG: ilo:IL2624 0.0045 atpE; F0F1-type ATP synthase, subunit c K02110; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. PREVCOP_04527, InterPro:IPR006153, EFB36105]

Ruminococcus torques ATCC27756

EDK23798.1 - KEGG: ilo:IL2624 0.31 atpE; F0F1-type ATP synthase, subunit c; COG: COG4824 Phage-related holin (Lysis protein); Psort location: CytoplasmicMembrane, score: 9.99 [a.k.a. RUMTOR_02100, toxin secretion/phage lysis holin, GI:145846880]

Aneurinibacillus aneurinilyticus

ERI08418.1 - UPF0756 membrane protein HMPREF0083_03523; KEGG: bip:Bint_2489 0.0013 putative F0F1-type ATP synthase, subunit C; K02110 F-type H+-transporting ATPase subunit c; Psort location: CytoplasmicMembrane, score: 10.00 [a.k.a. HMPREF0083_03523, GI:542057226, IPR007382]

Roseobacter sp. GAI101

EEB83878.1 - H+-transporting two-sector ATPase, B/B' subunit; [C] COG0711 F0F1-type ATP synthase, subunit b; Belongs to the ATPase B chain family [a.k.a. RGAI101_1028, EEB83878, H+-transporting two-sector ATPase, B/B' subunit]

Methylobacter tundripaludum

Mettu_0385 - TIGRFAM: ATPase, F1 complex, beta subunit; HAMAP: ATPase, F1 complex, beta subunit; KEGG: mca:MCA1556 F0F1 ATP synthase subunit beta; PFAM: ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain; ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal; ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal [a.k.a. EGW21616.1, WP_006889595.1, InterPro:IPR000194]

Anaplasma marginale Maries

atpE - COG0636 AtpE F0F1-type ATP synthase c subunit/Archaeal/vacuolar-type H+-ATPase subunit K [a.k.a. AM1112, AAV86964.1, GI:56388377]

Cyanobium sp. PCC7001

atpK - [C] COG0636 F0F1-type ATP synthase, subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [a.k.a. CPCC7001_1678, EDY38799.1, B5IQ69_9CYAN]

Roseobacter sp. GAI101

EEB84890.1 - [C] COG0355 F0F1-type ATP synthase, epsilon subunit (mitochondrial delta subunit) [a.k.a. RGAI101_2040, EEB84890, Alternate F1F0 ATPase, F1 subunit epsilon]

Sphingomonas sp. S17

EGI55145.1 - [C] COG0355 F0F1-type ATP synthase, epsilon subunit (mitochondrial delta subunit) [a.k.a. SUS17_2020, GI:332013082, EGI55145]

Aquamicrobium defluvii

BG36_14115 - ATP synthase F0F1 subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology [a.k.a. EXL02707.1, WP_035030735.1, GI:590076371]

Natrialba magadii

Nmag_4181 - Uncharacterized protein; KEGG: tgr:Tgr7_3310 F0F1 ATP synthase subunit C [a.k.a. C500_15105, ADD07693.1, GI:289533344]

Pontibacillus chungwhensis

N780_16015 - ATP synthase F0F1 subunit C; Derived by automated computational analysis using gene prediction method: Protein Homology [a.k.a. KGP91858.1, A0A0A2UYN6_9BACI, 701633028]

Herbaspirillum seropedicae

atpI - F0F1-type ATP synthase, subunit I protein; C - Energy production and conversion [a.k.a. Hsero_4369, ADJ65837.1, GI:300076438]

Cyanobium sp. PCC7001

EDY39513.1 - Uncharacterized protein; [C] COG0711 F0F1-type ATP synthase, subunit b [a.k.a. CPCC7001_2394, EDY39513, 197626954]

Gammaproteobacteria bacterium HTCC2148

EEB77229.1 - Uncharacterized protein; [C] COG0356 F0F1-type ATP synthase, subunit a [a.k.a. GPB2148_370, 214036555, EEB77229]

Gammaproteobacteria bacterium HTCC2148

atpI - [C] COG3312 F0F1-type ATP synthase, subunit I [a.k.a. GPB2148_397, EEB77256.1, EEB77256]

Gammaproteobacteria bacterium NOR53

NOR53_3395 - Uncharacterized protein; [C] COG3312 F0F1-type ATP synthase, subunit I [a.k.a. EED31968.1, conserved hypothetical protein, GI:219675602]

Pseudomonas sp. UW4

atpI - [C] COG3312 F0F1-type ATP synthase, subunit I [a.k.a. PputUW4_05434, AFY22623.1, ATP synthase subunit I]

Sphingomonas sp. S17

EGI53369.1 - [C] COG0711 F0F1-type ATP synthase, subunit b [a.k.a. SUS17_3823, EGI53369, ATP synthase B/B' CF family protein]

Sphingomonas sp. S17

EGI53344.1 - [C] COG0711 F0F1-type ATP synthase, subunit b [a.k.a. SUS17_3824, GI:332011253, EGI53344]

Sphingomonas sp. S17

atpB - [C] COG0356 F0F1-type ATP synthase, subunit a [a.k.a. EGI53348.1, SUS17_3826, EGI53348]

Asticcacaulis biprosthecum

fliI - Flagellar protein export ATPase FliI; [C] COG0056 F0F1-type ATP synthase, alpha subunit [a.k.a. ABI_28400, EGF91424.1, WP_006273626.1]

Gammaproteobacteria bacterium NOR53

fliI - Flagellar protein export ATPase FliI; [C] COG0056 F0F1-type ATP synthase, alpha subunit [a.k.a. NOR53_85, EED30883.1, B8KP49]

Rhodobacteraceae bacterium HTCC2083

fliI - [C] COG0056 F0F1-type ATP synthase, alpha subunit [a.k.a. RB2083_2961, EDZ43446.1, WP_009830276.1]

Rhodobacterales bacterium Y4I

fliI - [C] COG0055 F0F1-type ATP synthase, beta subunit [a.k.a. RBY4I_483, EDZ45276.1, flagellum-specific ATP synthase]

Roseobacter sp. GAI101

atpG_1 - [C] COG0224 F0F1-type ATP synthase, gamma subunit [a.k.a. RGAI101_2174, EEB85024.1, B7RJ27_9RHOB]

Roseobacter sp. GAI101

fliI - [C] COG0056 F0F1-type ATP synthase, alpha subunit [a.k.a. RGAI101_712, EEB83563.1, flagellum-specific ATP synthase]

Sphingomonas sp. S17

atpD - [C] COG0055 F0F1-type ATP synthase, beta subunit [a.k.a. EGI55139.1, SUS17_2022, ATP synthase F1, beta subunit]

Sphingomonas sp. S17

atpG - [C] COG0224 F0F1-type ATP synthase, gamma subunit [a.k.a. EGI55292.1, SUS17_2024, 332013229]

Sphingomonas sp. S17

atpA - [C] COG0056 F0F1-type ATP synthase, alpha subunit [a.k.a. SUS17_3761, EGI53399.1, GI:332011310]

Sphingomonas sp. S17

atpH - [C] COG0712 F0F1-type ATP synthase, delta subunit (mitochondrial oligomycin sensitivity protein) [a.k.a. SUS17_3762, EGI53400.1, GI:332011311]

Synechococcus sp. PCC7335

S7335_777 - [C] COG0224 F0F1-type ATP synthase, gamma subunit [a.k.a. EDX83597.1, GI:196188632, B4WTA3]

Streptomyces mobaraensis

H340_11635 - Lanthionine synthetase C-like protein; COG0056 F0F1-type ATP synthase, alpha subunit [a.k.a. EMF00358.1, M3B312, EMF00358]

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