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yfiH yfiH cbdB cbdB cbdA cbdA cueO cueO cyoB cyoB cyoA cyoA cydA cydA cydB cydB cydX cydX yedZ yedZ
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
yfiHUPF0124 family protein; Multicopper oxidase with polyphenol oxidase activity. Is able to oxidize syringaldazine and 2,2'-azino-bis(3-ethylbenzthiazoline-6- sulfonic acid) (ABTS) in vitro. The physiological substrate and role of YfiH is not known. (243 aa)
cbdBCytochrome bd-II oxidase, subunit II; A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (378 aa)
cbdACytochrome bd-II oxidase, subunit I; A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (514 aa)
cueOMulticopper oxidase (laccase); Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm. (516 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Protons are probably pumped via D- and K- channels found in this subunit. (663 aa)
cyoACytochrome o ubiquinol oxidase subunit II; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. (315 aa)
cydACytochrome d terminal oxidase, subunit I; A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (522 aa)
cydBCytochrome d terminal oxidase, subunit II; A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (379 aa)
cydXCytochrome d (bd-I) ubiquinol oxidase subunit X; Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap. (37 aa)
yedZInner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] (211 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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