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nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF atpD atpD atpC atpC yjgP yjgP yjgQ yjgQ znuC znuC emrE emrE cysW cysW cysA cysA znuB znuB yhbG yhbG folK folK cyoD cyoD cyoC cyoC atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB sdhC sdhC sdhA sdhA sdhB sdhB msbA msbA lolE lolE nuoE nuoE lolD lolD lolC lolC atpG atpG nuoN nuoN nuoA nuoA nuoB nuoB nuoCD nuoCD nuoL nuoL
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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nuoKNADH dehydrogenase I chain K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (100 aa)
nuoJNADH dehydrogenase I chain J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (183 aa)
nuoINADH dehydrogenase I chain I, 2Fe-2S ferredoxin-related; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (181 aa)
nuoHNADH dehydrogenase I chain H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (323 aa)
nuoGNADH dehydrogenase I chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family. (919 aa)
nuoFNADH dehydrogenase I chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (443 aa)
atpDATP synthase, F1 sector, beta-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (462 aa)
atpCATP synthase, F1 sector, epsilon-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (144 aa)
yjgPPutative transmembrane protein, transport; Ortholog to Escherichia coli bnum: b4261; MultiFun: Cell structure 6.1; Transport 4. (373 aa)
yjgQPutative transmembrane protein, transport; Ortholog to Escherichia coli bnum: b4262; MultiFun: Cell structure 6.1. (357 aa)
znuCHigh-affinity Zn transport protein (ABC superfamily, atp_bind); Ortholog to Escherichia coli bnum: b1858; MultiFun: Metabolism 1.5.3.12; Transport 4.3.A.1.a, 4.S.191. (215 aa)
emrEAuxillary multidrug transport protein (SMR family); Ortholog to Escherichia coli bnum: b0543; MultiFun: Cell processes 5.6.4; Cell structure 6.1; Transport 4.2.A.7, 4.S.126. (109 aa)
cysWThiosulfate permease W protein (ABC superfamily, membrane); Ortholog to Escherichia coli bnum: b2423; MultiFun: Cell structure 6.1; Metabolism 1.8.2; Transport 4.3.A.1.m, 4.S.178. (286 aa)
cysASulfate permease A protein, chromate resistance (ABC superfamily, atp_bind); Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. (355 aa)
znuBHigh-affinity Zn transport protein (ABC superfamily, membrane); Ortholog to Escherichia coli bnum: b1859; MultiFun: Cell structure 6.1; Transport 4.3.A.1.m, 4.S.191. (286 aa)
yhbGPutative transport protein (ABC superfamily, atp_bind); Ortholog to Escherichia coli bnum: b3201; MultiFun: Transport 4.3.A.1.a. (241 aa)
folK2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase; Ortholog to Escherichia coli bnum: b0142; MultiFun: Metabolism 1.5.3.2. (164 aa)
cyoDCytochrome o ubiquinol oxidase, subunit IV; Ortholog to Escherichia coli bnum: b0429; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2. (100 aa)
cyoCCytochrome o ubiquinol oxidase, subunit III; Ortholog to Escherichia coli bnum: b0430; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.4.2; Transport 4.3.D.4, 4.S.82. (195 aa)
atpAATP synthase, F1 sector, alpha-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (513 aa)
atpHATP synthase, F1 sector, delta-subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (181 aa)
atpFATP synthase, F0 sector, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (160 aa)
atpEATP synthase, F0 sector, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (79 aa)
atpBATP synthase, F0 sector, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (269 aa)
sdhCSuccinate dehydrogenase cytochrome b-556 subunit; Ortholog to Escherichia coli bnum: b0721; MultiFun: Cell structure 6.1; Metabolism 1.3.4, 1.3.6, 1.4.1, 1.4.3, 1.6.15.1. (135 aa)
sdhASuccinate dehydrogenase catalytic and flavoprotein subunit; Ortholog to Escherichia coli bnum: b0723; MultiFun: Metabolism 1.3.4, 1.3.6, 1.4.1; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (594 aa)
sdhBSuccinate dehydrogenase iron-sulfur protein; Ortholog to Escherichia coli bnum: b0724; MultiFun: Metabolism 1.3.4, 1.3.6, 1.4.1. (248 aa)
msbALipid transport protein; Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. (584 aa)
lolETransport protein of outer membrane lipoproteins (ABC superfamily, membrane); Ortholog to Escherichia coli bnum: b1118; MultiFun: Cell structure 6.1; Transport 4.3.A.1.m, 4.S.106. (411 aa)
nuoENADH dehydrogenase I chain E; Ortholog to Escherichia coli bnum: b2285; MultiFun: Metabolism 1.3.6; Metabolism 1.3.7, 1.4.1; Transport 4.3.D.1, 4.S.130. (173 aa)
lolDTransport protein of outer membrane lipoproteins (ABC superfamily, atp_bind); Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. (233 aa)
lolCTransport protein of outer membrane lipoproteins (ABC superfamily, membrane); Ortholog to Escherichia coli bnum: b1116; MultiFun: Cell structure 6.1; Transport 4.3.A.1.m, 4.S.106. (401 aa)
atpGATP synthase, F1 sector, gamma-subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (288 aa)
nuoNNADH dehydrogenase I chain N, membrane subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (497 aa)
nuoANADH dehydrogenase I chain A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (146 aa)
nuoBNADH dehydrogenase I chain B, binds FeS cluster N2; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (236 aa)
nuoCDNADH dehydrogenase I chain C, D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (596 aa)
nuoLNADH dehydrogenase I chain L, membrane subunit; Ortholog to Escherichia coli bnum: b2278; MultiFun: Cell structure 6.1; Metabolism 1.3.6, 1.3.7, 1.4.1; Transport 4.3.D.1, 4.S.130. (628 aa)
Your Current Organism:
Blochmannia pennsylvanicus
NCBI taxonomy Id: 291272
Other names: C. Blochmannia pennsylvanicus str. BPEN, Candidatus Blochmannia pennsylvanicus BPEN, Candidatus Blochmannia pennsylvanicus str. BPEN, Candidatus Blochmannia pennsylvanicus strain BPEN
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