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
qoxBQoxB, Quinol oxidase subunit II; IMG reference gene:2512956600; PFAM: Cytochrome C oxidase subunit II, periplasmic domain; non-canonical start codon; truncated by 90 aa. (217 aa)    
Predicted Functional Partners:
qoxA
QoxA, Quinol oxidase subunit I; IMG reference gene:2512956599; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
coxIII
IMG reference gene:2512953738; PFAM: Cytochrome c oxidase subunit III.
 
 0.998
RSP_0117
IMG reference gene:2512955108; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.996
coxI
Cytochrome c oxidase, aa3 type, 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.
 
 0.996
fbcB
Cytochrome b; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 0.993
nuoCD
NADH dehydrogenase subunit C; 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.
   
 
 0.984
cox10
Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
 
  
 0.974
fbcF
Ubiquinol-cytochrome C reductase, iron-sulfur protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
  
 0.949
RSP_0111
IMG reference gene:2512955102; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; old pseudo; frameshift corrected.
  
 
 0.930
nuoH1
Putative NADH dehydrogenase I chain H; 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. This subunit may bind ubiquinone.
  
 
 0.927
Your Current Organism:
Rhodobacter sphaeroides 241
NCBI taxonomy Id: 272943
Other names: R. sphaeroides 2.4.1, Rhodobacter sphaeroides 2.4.1, Rhodobacter sphaeroides ATCC 17023, Rhodobacter sphaeroides ATH 2.4.1, Rhodobacter sphaeroides str. 2.4.1, Rhodobacter sphaeroides strain 2.4.1
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