STRINGSTRING
GCA_000285535_00091 GCA_000285535_00091 GCA_000285535_04381 GCA_000285535_04381 GCA_000285535_04380 GCA_000285535_04380 E1I69_01595 E1I69_01595 E1I69_01950 E1I69_01950 E1I69_01955 E1I69_01955 E1I69_01960 E1I69_01960 E1I69_02220 E1I69_02220 E1I69_02225 E1I69_02225 E1I69_02385 E1I69_02385 sdhA sdhA sdhB sdhB ctaB-2 ctaB-2 E1I69_11880 E1I69_11880 E1I69_11885 E1I69_11885 E1I69_10180 E1I69_10180 qoxA qoxA qoxB qoxB qoxC qoxC qoxD qoxD E1I69_09900 E1I69_09900 E1I69_18325 E1I69_18325 E1I69_18330 E1I69_18330 E1I69_19405 E1I69_19405 atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC nuoA nuoA nuoB nuoB E1I69_16710 E1I69_16710 nuoD nuoD nuoH nuoH nuoI nuoI E1I69_16690 E1I69_16690 nuoK nuoK E1I69_16680 E1I69_16680 E1I69_16675 E1I69_16675 nuoN nuoN GCA_000285535_02429 GCA_000285535_02429 GCA_000285535_02117 GCA_000285535_02117 ppaX ppaX E1I69_19755 E1I69_19755 E1I69_19770 E1I69_19770 E1I69_19855 E1I69_19855 E1I69_19860 E1I69_19860 E1I69_15875 E1I69_15875 E1I69_15825 E1I69_15825 E1I69_15820 E1I69_15820 E1I69_22635 E1I69_22635 ctaA ctaA ctaB ctaB coxB coxB ctaD ctaD E1I69_03465 E1I69_03465 ctaF ctaF E1I69_03855 E1I69_03855 rbfA rbfA E1I69_04395 E1I69_04395 E1I69_04470 E1I69_04470 E1I69_04475 E1I69_04475 GCA_000285535_00619 GCA_000285535_00619 ppaC ppaC E1I69_06775 E1I69_06775 E1I69_21140 E1I69_21140
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
GCA_000285535_00091Unannotated protein. (265 aa)
GCA_000285535_04381Unannotated protein. (516 aa)
GCA_000285535_04380Unannotated protein. (871 aa)
E1I69_01595Unannotated protein. (270 aa)
E1I69_01950Unannotated protein. (169 aa)
E1I69_01955Unannotated protein. (224 aa)
E1I69_01960Unannotated protein; Component of the menaquinol-cytochrome c reductase complex. (255 aa)
E1I69_02220Unannotated protein; Belongs to the heme-copper respiratory oxidase family. (550 aa)
E1I69_02225Unannotated protein. (173 aa)
E1I69_02385Unannotated protein. (202 aa)
sdhAUnannotated protein. (586 aa)
sdhBUnannotated protein. (252 aa)
ctaB-2Unannotated protein; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (300 aa)
E1I69_11880Unannotated protein. (157 aa)
E1I69_11885Unannotated protein. (563 aa)
E1I69_10180Unannotated protein. (175 aa)
qoxAUnannotated protein; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. (303 aa)
qoxBUnannotated protein; Belongs to the heme-copper respiratory oxidase family. (649 aa)
qoxCUnannotated protein. (198 aa)
qoxDUnannotated protein. (93 aa)
E1I69_09900Unannotated protein. (348 aa)
E1I69_18325Unannotated protein. (112 aa)
E1I69_18330Unannotated protein. (496 aa)
E1I69_19405Unannotated protein. (125 aa)
atpBUnannotated protein; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (244 aa)
atpEUnannotated protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (72 aa)
atpFUnannotated protein; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (174 aa)
atpHUnannotated protein; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (178 aa)
atpAUnannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (503 aa)
atpGUnannotated protein; 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. (285 aa)
atpDUnannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (504 aa)
atpCUnannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. (134 aa)
nuoAUnannotated protein; 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 a menaquinone. 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. (125 aa)
nuoBUnannotated protein; 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 a menaquinone. 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. (170 aa)
E1I69_16710Unannotated protein. (149 aa)
nuoDUnannotated protein; 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 a menaquinone. 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 49 kDa subunit family. (366 aa)
nuoHUnannotated protein; 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. (333 aa)
nuoIUnannotated protein; 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. (139 aa)
E1I69_16690Unannotated protein; 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. (171 aa)
nuoKUnannotated protein; 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 a menaquinone. 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. (104 aa)
E1I69_16680Unannotated protein. (622 aa)
E1I69_16675Unannotated protein. (503 aa)
nuoNUnannotated protein; 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 a menaquinone. 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. (502 aa)
GCA_000285535_02429Unannotated protein. (202 aa)
GCA_000285535_02117Unannotated protein. (357 aa)
ppaXUnannotated protein; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool. (213 aa)
E1I69_19755Unannotated protein. (355 aa)
E1I69_19770Unannotated protein. (405 aa)
E1I69_19855Unannotated protein. (493 aa)
E1I69_19860Unannotated protein. (113 aa)
E1I69_15875Unannotated protein. (413 aa)
E1I69_15825Unannotated protein. (174 aa)
E1I69_15820Unannotated protein. (495 aa)
E1I69_22635Unannotated protein. (521 aa)
ctaAUnannotated protein; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 1 subfamily. (356 aa)
ctaBUnannotated protein; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (312 aa)
coxBUnannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (358 aa)
ctaDUnannotated protein; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (624 aa)
E1I69_03465Unannotated protein. (204 aa)
ctaFUnannotated protein. (108 aa)
E1I69_03855Unannotated protein. (896 aa)
rbfAUnannotated protein; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. (121 aa)
E1I69_04395Unannotated protein; Belongs to the peptidase M16 family. (413 aa)
E1I69_04470Unannotated protein. (426 aa)
E1I69_04475Unannotated protein. (272 aa)
GCA_000285535_00619Unannotated protein. (40 aa)
ppaCUnannotated protein. (311 aa)
E1I69_06775Unannotated protein. (525 aa)
E1I69_21140Unannotated protein. (394 aa)
Your Current Organism:
Bacillus timonensis
NCBI taxonomy Id: 1033734
Other names: B. timonensis, Bacillus sp. 10403023, CSUR P162, DSM 25372, strain 10403023, strain MM10403188
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