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nuoF nuoF cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA nuoN nuoN nuoM nuoM nuoL nuoL nuoJ nuoJ hycC hycC hycE hycE hycG hycG hyfI hyfI hyfG hyfG hyfD hyfD hyfB hyfB nuoA nuoA nuoB nuoB nuoC nuoC nuoG nuoG
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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:
nuoFNADH dehydrogenase I 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. (445 aa)
cyoDCytochrome o ubiquinol oxidase subunit IV; 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 (By similarity). (109 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Residues 1 to 204 of 204 are 99.50 pct identical to residues 1 to 204 of 204 from Escherichia coli K-12 Strain MG1655: B0430. (204 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 (By similarity). (663 aa)
cyoACytochrome o ubiquinol oxidase subunit II; Residues 1 to 315 of 315 are 99.04 pct identical to residues 1 to 315 of 315 from Escherichia coli K-12 Strain MG1655: B0432. (315 aa)
nuoNNADH dehydrogenase I 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. (425 aa)
nuoMNADH dehydrogenase I chain M; 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 (By similarity); Belongs to the complex I subunit 4 family. (509 aa)
nuoLNADH dehydrogenase I chain L; Residues 1 to 613 of 613 are 99.83 pct identical to residues 1 to 613 of 613 from Escherichia coli K-12 Strain MG1655: B2278. (613 aa)
nuoJNADH dehydrogenase I chain J; 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 (By similarity); Belongs to the complex I subunit 6 family. (184 aa)
hycCMembrane-spanning protein of hydrogenase 3 (part of FHL complex); Residues 1 to 608 of 608 are 99.17 pct identical to residues 1 to 608 of 608 from Escherichia coli K-12 Strain MG1655: B2723. (608 aa)
hycELarge subunit of hydrogenase 3 (part of FHL complex); Residues 1 to 569 of 569 are 99.82 pct identical to residues 1 to 569 of 569 from Escherichia coli K-12 Strain MG1655: B2721. (569 aa)
hycGHydrogenase activity; Residues 1 to 255 of 255 are 99.60 pct identical to residues 1 to 255 of 255 from Escherichia coli K-12 Strain MG1655: B2719. (255 aa)
hyfIHydrogenase 4 Fe-S subunit; Residues 1 to 252 of 252 are 99.20 pct identical to residues 1 to 252 of 252 from Escherichia coli K-12 Strain MG1655: B2489. (252 aa)
hyfGHydrogenase 4 subunit; Residues 1 to 571 of 571 are 96.84 pct identical to residues 1 to 555 of 555 from Escherichia coli K-12 Strain MG1655: B2487. (571 aa)
hyfDHydrogenase 4 membrane subunit; Residues 1 to 479 of 479 are 99.58 pct identical to residues 1 to 479 of 479 from Escherichia coli K-12 Strain MG1655: B2484. (479 aa)
hyfBHydrogenase 4 membrane subunit; Residues 1 to 672 of 672 are 98.95 pct identical to residues 1 to 672 of 672 from Escherichia coli K-12 Strain MG1655: B2482. (672 aa)
nuoANADH dehydrogenase I 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. (147 aa)
nuoBNADH dehydrogenase I 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. (220 aa)
nuoCNADH dehydrogenase I chain C, 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
nuoGNADH dehydrogenase I chain G; 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 (By similarity). (910 aa)
Your Current Organism:
Escherichia coli O157H7 EDL933
NCBI taxonomy Id: 155864
Other names: E. coli O157:H7 str. EDL933, Escherichia coli O157:H7 EDL933, Escherichia coli O157:H7 str. EDL933, Escherichia coli O157:H7 strain EDL933
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