STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Bsel_2115PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: gur:Gura_2379 Rieske (2Fe-2S) domain-containing protein. (167 aa)    
Predicted Functional Partners:
Bsel_1624
Cytochrome 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).
 
 0.999
Bsel_2113
Cytochrome b subunit of the bc complex-like protein; Component of the menaquinol-cytochrome c reductase complex.
 
 0.999
Bsel_2114
PFAM: Cytochrome b/b6 domain; KEGG: petB; cytochrome B6.
 
 0.999
nuoI
NADH-quinone oxidoreductase, chain I; 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.
  
 0.989
Bsel_1625
Cytochrome 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.
 
 0.988
nuoD
NADH dehydrogenase I, D 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; Belongs to the complex I 49 kDa subunit family.
   
 0.986
Bsel_1079
PFAM: cytochrome c class I; KEGG: smt:Smal_1045 cytochrome c class I.
 
 
 0.980
Bsel_2343
PFAM: cytochrome c class I; KEGG: cco:CCC13826_0726 cytochrome c oxidase, Cbb3-type, subunit III.
 
 
 0.979
Bsel_3148
PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: scl:sce9060 NADH dehydrogenase (ubiquinone).
   
 
 0.970
nuoB
NADH-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.
  
 0.970
Your Current Organism:
Bacillus selenitireducens
NCBI taxonomy Id: 439292
Other names: Bacillus selenitireducens MLS10, [. selenitireducens MLS10, [Bacillus] selenitireducens MLS10
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.