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ykgC ykgC dmsC dmsC lpd lpd grxB grxB dsbB dsbB ynfE ynfE ynfF ynfF ynfH ynfH ydhD ydhD ydjX ydjX ydjZ ydjZ msrB msrB yebR yebR yedY yedY ccmG ccmG trxC trxC nrdH nrdH cysH cysH cysI cysI cysJ cysJ dsbC dsbC dsbA dsbA dsbI dsbI gor gor grxC grxC trxA trxA dsbA-2 dsbA-2 dipZ dipZ msrA msrA dmsA dmsA trxB trxB grxA grxA ahpF ahpF ahpC ahpC
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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
Others
textmining
co-expression
protein homology
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ykgCPutative pyridine nucleotide-disulfide oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (441 aa)
dmsCDimethyl sulfoxide reductase, anaerobic, subunit C; Function experimentally demonstrated in the studied species; enzyme. (287 aa)
lpdLipoamide dehydrogenase, E3 component is part of three enzyme complexes; Function experimentally demonstrated in the studied species; enzyme. (474 aa)
grxBGlutaredoxin 2 (Grx2); Function experimentally demonstrated in the studied species; carrier. (215 aa)
dsbBOxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (176 aa)
ynfEOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa)
ynfFOxidoreductase subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (807 aa)
ynfHOxidoreductase, membrane subunit; Function experimentally demonstrated in the studied species; membrane component. (284 aa)
ydhDMonothiol glutaredoxin; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glutaredoxin family. Monothiol subfamily. (115 aa)
ydjXConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative membrane component. (236 aa)
ydjZConserved hypothetical protein; Homologs of previously reported genes of unknown function; putative membrane component. (235 aa)
msrBMethionine sulfoxide reductase B; Function experimentally demonstrated in the studied species; enzyme; Belongs to the MsrB Met sulfoxide reductase family. (137 aa)
yebRConserved hypothetical protein; Homologs of previously reported genes of unknown function. (183 aa)
yedYExported heme-molybdoenzyme molybdopterin-containing subunit YedY; 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 generated by the host defense mechanisms. 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 [...] (334 aa)
ccmGPeriplasmic thioredoxin of cytochrome c-type biogenesis; Function experimentally demonstrated in the studied species; enzyme. (185 aa)
trxCThioredoxin 2; Function experimentally demonstrated in the studied species; carrier; Belongs to the thioredoxin family. (139 aa)
nrdHGlutaredoxin-like protein; Function experimentally demonstrated in the studied species; putative carrier. (81 aa)
cysH3'-phosphoadenosine 5'-phosphosulfate reductase; Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily. (244 aa)
cysISulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (570 aa)
cysJSulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. (599 aa)
dsbCProtein disulfide isomerase II; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (236 aa)
dsbAThiol:disulfide interchange protein dsbA precursor; Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT. (222 aa)
dsbIPutative protein-disulfide oxidoreductase; Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT. (223 aa)
gorGlutathione oxidoreductase; Function experimentally demonstrated in the studied species; carrier. (450 aa)
grxCGlutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. (83 aa)
trxAFunction experimentally demonstrated in the studied species; carrier; Belongs to the thioredoxin family. (109 aa)
dsbA-2Periplasmic protein disulfide isomerase I; Function experimentally demonstrated in the studied species; enzyme. (208 aa)
dipZFragment of putative transcriptional regulator (part 1); Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (565 aa)
msrAMethionine sulfoxide reductase A; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. (212 aa)
dmsADimethyl sulfoxide reductase, anaerobic, subunit A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (814 aa)
trxBThioredoxin reductase, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (321 aa)
grxAGlutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); Function experimentally demonstrated in the studied species; carrier. (85 aa)
ahpFAlkyl hydroperoxide reductase, F52a subunit, FAD/NAD(P)-binding; Function experimentally demonstrated in the studied species; enzyme. (521 aa)
ahpCAlkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
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