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ctaF ctaF qoxA qoxA qoxB qoxB qoxC qoxC ctaD ctaD Aflv_1360 Aflv_1360 Aflv_1863 Aflv_1863 ctaE ctaE ctaD-2 ctaD-2 ctaC ctaC mrpD mrpD nuoN nuoN nuoM nuoM nuoL nuoL nuoJ nuoJ nuoC nuoC nuoB nuoB nuoA nuoA ahpF ahpF
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:
ctaFCytochrome caa3 oxidase (subunit IV). (110 aa)
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)
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_1863Predicted membrane protein. (154 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)
mrpDMultisubunit Na+/H+ antiporter, D subunit. (490 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)
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)
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)
ahpFAlkyl hydroperoxide reductase large subunit. (509 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
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