STRINGSTRING
Bsel_3142 Bsel_3142 Bsel_3281 Bsel_3281 nuoA nuoA nuoB nuoB Bsel_3148 Bsel_3148 Bsel_3144 Bsel_3144 Bsel_1624 Bsel_1624 Bsel_1625 Bsel_1625 Bsel_3141 Bsel_3141 nuoN nuoN Bsel_2389 Bsel_2389 Bsel_2058 Bsel_2058 Bsel_1628 Bsel_1628 Bsel_1627 Bsel_1627
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
Others
textmining
co-expression
protein homology
Your Input:
Bsel_3142TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; KEGG: gur:Gura_4233 proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH/Ubiquinone/plastoquinone (complex I); NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein. (642 aa)
Bsel_3281PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; HI0933 family protein; KEGG: vpa:VP1199 putative glutamate synthase, small chain. (594 aa)
nuoANADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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. (124 aa)
nuoBNADH-quinone oxidoreductase, B subunit; 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. (175 aa)
Bsel_3148PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: scl:sce9060 NADH dehydrogenase (ubiquinone). (159 aa)
Bsel_3144NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (165 aa)
Bsel_1624Cytochrome c 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). (345 aa)
Bsel_1625Cytochrome c 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. (613 aa)
Bsel_3141KEGG: gme:Gmet_3343 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (512 aa)
nuoNProton-translocating NADH-quinone oxidoreductase, 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 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. (485 aa)
Bsel_2389PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: tgr:Tgr7_2525 NADH dehydrogenase (quinone). (497 aa)
Bsel_2058PFAM: protein of unknown function DUF420; KEGG: scl:sce6560 hypothetical protein. (178 aa)
Bsel_1628PFAM: protein of unknown function DUF420; KEGG: ank:AnaeK_0947 protein of unknown function DUF420. (159 aa)
Bsel_1627PFAM: cytochrome C oxidase subunit IV; KEGG: rme:Rmet_5790 cytochrome c oxidase subunit IV. (115 aa)
Your Current Organism:
Bacillus selenitireducens
NCBI taxonomy Id: 439292
Other names: Bacillus selenitireducens MLS10, [. selenitireducens MLS10, [Bacillus] selenitireducens MLS10
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