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atpB atpB atpE atpE atpF atpF atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC ctaD ctaD ctaC ctaC petA petA petB petB petC petC Rta_08967 Rta_08967 Rta_11920 Rta_11920 Rta_18430 Rta_18430 ppa ppa ppk ppk Rta_25140 Rta_25140 Rta_25150 Rta_25150 sdhB sdhB nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA atpE-2 atpE-2 Rta_28080 Rta_28080 Rta_28090 Rta_28090 sdhA sdhA sdhB-2 sdhB-2 ctaB ctaB Rta_33670 Rta_33670 ctaE ctaE ctaG ctaG ctaD-2 ctaD-2 ctaC-2 ctaC-2
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:
atpBCandidate F-ATPase, A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (305 aa)
atpECandidate F-ATPase, C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (82 aa)
atpFCandidate F-ATPase, B chain; 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. (156 aa)
atpHCandidate F-ATPase, delta chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During 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. (176 aa)
atpACandidate F-ATPase, alpha chain; 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. (517 aa)
atpGCandidate F-ATPase, gamma chain; 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. (294 aa)
atpDCandidate F-ATPase, beta chain; 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. (469 aa)
atpCCandidate F-ATPase, epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. (142 aa)
ctaDCandidate Cytochrome c oxidase polypeptide I (Cytochrome AA3 subunit 1). (860 aa)
ctaCCandidate Cytochrome c oxidase polypeptide II precursor (Cytochrome aa3 subunit 2). (276 aa)
petACandidate Ubiquinol-cytochrome c reductase iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (198 aa)
petBCandidate cytochrome b, membrane protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (471 aa)
petCCandidate Cytochrome c1 precursor. (256 aa)
Rta_08967Candidate membrane protein. (542 aa)
Rta_11920NADH dehydrogenase-like protein. (450 aa)
Rta_18430Succinate dehydrogenase, flavoprotein subunit (Fumarate reductase)-like protein. (426 aa)
ppaPyrophosphate phosphohydrolase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (178 aa)
ppkATP- polyphosphate phosphotransferase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (706 aa)
Rta_25140Cytochrome d ubiquinol oxidase subunit I-like protein. (475 aa)
Rta_25150Cytochrome bd-II oxidase subunit II-like protein. (348 aa)
sdhBCandidate succinate dehydrogenase iron-sulfur protein. (234 aa)
nuoNCandidate NADH:ubiquinone oxidoreductase subunit 14 or 2, chain N; 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. (495 aa)
nuoMCandidate NADH:ubiquinone oxidoreductase subunit 13 or 4, chain M. (491 aa)
nuoLCandidate NADH:ubiquinone oxidoreductase subunit 12 or 5, chain L. (685 aa)
nuoKCandidate NADH:ubiquinone oxidoreductase subunit 11 or 4L, 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. (102 aa)
nuoJCandidate NADH:ubiquinone oxidoreductase subunit 10 or 6, 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. (218 aa)
nuoICandidate NADH:ubiquinone oxidoreductase subunit 9 or 23 kDa subunit, chain I; 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. (172 aa)
nuoHCandidate NADH:ubiquinone oxidoreductase subunit 8 or 1, 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. (360 aa)
nuoGCandidate NADH:ubiquinone oxidoreductase subunit 3 or 75 kDa subunit, 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. (702 aa)
nuoFCandidate NADH:ubiquinone oxidoreductase subunit 1 or 51 kDa subunit, 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. (455 aa)
nuoECandidate NADH:ubiquinone oxidoreductase subunit 2 or 24 kDa subunit, chain E. (162 aa)
nuoDCandidate NADH:ubiquinone oxidoreductase subunit 4 or 49 kDa subunit, chain 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; Belongs to the complex I 49 kDa subunit family. (417 aa)
nuoCCandidate NADH:ubiquinone oxidoreductase subunit 5 or 30 kDa subunit, chain C; 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 30 kDa subunit family. (212 aa)
nuoBCandidate NADH:ubiquinone oxidoreductase subunit 6 or 20 kDa subunit, chain B; 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. (159 aa)
nuoACandidate NADH:ubiquinone oxidoreductase subunit 7 or 3, 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. (123 aa)
atpE-2ATP synthase C chain-like 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. (80 aa)
Rta_28080Succinate dehydrogenase cytochrome b-556 subunit-like protein. (148 aa)
Rta_28090Succinate dehydrogenase hydrophobic membrane anchor protein-like protein. (121 aa)
sdhACandidate succinate dehydrogenase flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (602 aa)
sdhB-2Candidate succinate dehydrogenase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (234 aa)
ctaBCandidate protoheme IX farnesyltransferase (Heme O synthase), membrane 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. (289 aa)
Rta_33670Cytochrome AA3 controlling protein, membrane protein-like protein. (397 aa)
ctaEOxidase AA(3) subunit 3; membrane protein. (293 aa)
ctaGCandidate cytochrome C oxidase assembly protein. (195 aa)
ctaD-2Candidate cytochrome c oxidase polypeptide I (Cytochrome AA3 subunit 1); 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. (568 aa)
ctaC-2Candidate cytochrome c oxidase polypeptide II precursor (Cytochrome aa3 subunit 2); 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). (387 aa)
Your Current Organism:
Ramlibacter tataouinensis
NCBI taxonomy Id: 365046
Other names: Acidivorax sp. TTB310, Acidovorax sp. TTB310, R. tataouinensis TTB310, Ramlibacter tataouinensis TTB310, Ramlibacter tataouinensis str. TTB310, Ramlibacter tataouinensis strain TTB310
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