STRINGSTRING
qoxA qoxA qoxB qoxB qoxC qoxC qoxD qoxD cccA cccA ppa ppa qcrA qcrA qcrB qcrB qcrC qcrC ctaD ctaD Aflv_1360 Aflv_1360 Aflv_1450 Aflv_1450 Aflv_1537 Aflv_1537 Aflv_1538 Aflv_1538 Aflv_1863 Aflv_1863 ctaG ctaG ctaF ctaF ctaE ctaE ctaD-2 ctaD-2 ctaC ctaC ctaB ctaB ctaA ctaA Aflv_1966 Aflv_1966 spoIIQ spoIIQ spoIID spoIID Aflv_2688 Aflv_2688 Aflv_2689 Aflv_2689 nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB atpI atpI Aflv_2710 Aflv_2710 Aflv_2817 Aflv_2817
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:
qoxACytochrome aa3 quinol oxidase subunit II; 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. (324 aa)
qoxBCytochrome aa3 quinol oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (665 aa)
qoxCCytochrome aa3 quinol oxidase subunit III. (201 aa)
qoxDCytochrome aa3 quinol oxidase subunit IV. (99 aa)
cccACytochrome c550. (120 aa)
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (165 aa)
qcrAMenaquinol:cytochrome c oxidoreductase (iron-sulfur subunit). (180 aa)
qcrBMenaquinol:cytochrome c oxidoreductase (cytochrome b subunit). (224 aa)
qcrCMenaquinol-cytochrome c reductase cytochrome b/c subunit; Component of the menaquinol-cytochrome c reductase complex. (255 aa)
ctaDCytochrome c oxidase (b(o/a)3-type) chain I; Belongs to the heme-copper respiratory oxidase family. (549 aa)
Aflv_1360Cytochrome c oxidase (b(o/a)3-type) chain II. (157 aa)
Aflv_1450Cu2+-binding oxygen sensor (SCO1/SenC/PrrC family). (190 aa)
Aflv_1537Predicted Zn-dependent peptidase. (426 aa)
Aflv_1538Predicted Zn-dependent peptidase. (462 aa)
Aflv_1863Predicted membrane protein. (154 aa)
ctaGPredicted membrane protein. (291 aa)
ctaFCytochrome caa3 oxidase (subunit IV). (110 aa)
ctaECytochrome caa3 oxidase (subunit III). (206 aa)
ctaD-2Cytochrome caa3 oxidase (subunit I); 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. (622 aa)
ctaCCytochrome caa3 oxidase (subunit II); 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). (354 aa)
ctaBHeme O synthase (polyprenyltransferase); 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. (301 aa)
ctaAHeme A synthase (monooxygenase); 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. (316 aa)
Aflv_1966Predicted nucleoside-diphosphate-sugar epimerase. (234 aa)
spoIIQStage II sporulation protein Q required for completion of engulfment. (274 aa)
spoIIDStage II sporulation protein D required for complete dissolution of the asymmetric septum. (363 aa)
Aflv_2688Uncharacterized conserved protein. (255 aa)
Aflv_2689Uncharacterized small membrane protein. (82 aa)
nuoNNADH dehydrogenase subunit 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 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. (500 aa)
nuoMNADH dehydrogenase subunit M. (503 aa)
nuoLNADH dehydrogenase subunit L. (618 aa)
nuoKNADH dehydrogenase subunit 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 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. (103 aa)
nuoJNADH dehydrogenase subunit 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. (169 aa)
nuoINADH dehydrogenase subunit 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. (139 aa)
nuoHNADH dehydrogenase subunit 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. (333 aa)
nuoDNADH dehydrogenase subunit 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 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)
nuoCNADH dehydrogenase subunit C. (366 aa)
nuoBNADH dehydrogenase subunit 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 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. (177 aa)
nuoANADH dehydrogenase subunit 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 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. (132 aa)
atpCF0F1-type ATP synthase, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (134 aa)
atpDF0F1-type ATP synthase, 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. (473 aa)
atpGF0F1-type ATP synthase, 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. (290 aa)
atpAF0F1-type ATP synthase, 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. (507 aa)
atpHF0F1-type ATP synthase, 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. (178 aa)
atpFF0F1-type ATP synthase, subunit b; 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. (179 aa)
atpEF0F1-type ATP synthase, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (70 aa)
atpBF0F1-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (236 aa)
atpIMg2+ transporter AtpI (F0F1-ATP synthase subunit AtpI). (125 aa)
Aflv_2710Uncharacterized small membrane protein. (75 aa)
Aflv_2817Amino acid oxidase (deaminating). (504 aa)
Your Current Organism:
Anoxybacillus flavithermus
NCBI taxonomy Id: 491915
Other names: A. flavithermus WK1, Anoxybacillus flavithermus WK1, Anoxybacillus flavithermus str. WK1, Anoxybacillus flavithermus strain WK1
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.