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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
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[Homology]
Score
qcrBIn Corynebacterium glutamicum, a cytochrome aa3 terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC (cytochrome c1). Cytochrome aa3 is composed of subunits I (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits form the cytochrome bc1-aa3 supercomplex. (556 aa)    
Predicted Functional Partners:
ctaE
In Corynebacterium glutamicum, a cytochrome aa3 terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC (cytochrome c1). Cytochrome aa3 is composed of subunits I (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits form the cytochrome bc1-aa3 supercomplex.
 
 
 0.999
qcrC
Cytochrome bc1 complex cytochrome c1 subunit; In Corynebacterium glutamicum, a cytochrome aa3 terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC (cytochrome c1). Cytochrome aa3 is composed of subunits I (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits form the cytochrome bc1-aa3 supercomplex.
 
 0.999
qcrA
Cytochrome bc1 complex iron sulfur subunit; In Corynebacterium glutamicum, a cytochrome aa3 terminal oxidase (EC 1.9.3.1) receives electrons from a bc1 complex (EC 1.10.2.2). The bc1 complex is encoded by qcrA (Rieske iron-sulfur protein), qcrB (cytochrome B) and qcrC (cytochrome c1). Cytochrome aa3 is composed of subunits I (ctaD), II (ctaC), III (ctaE) and IV (ctaF). These subunits form the cytochrome bc1-aa3 supercomplex.
 
 0.999
ctaF
Cytochrome aa3 subunit 4; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
 
 
 0.999
ctaD
Cytochrome aa3 subunit 1; 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.
 
 
 0.999
ctaC
Cytochrome aa3 subunit 2; 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
AARI_10740
Putative M16 family peptidase; Identified by match to PF05193 and PF00675. These metallopeptidases belong to MEROPS peptidase family M16 (clan ME). They also include proteins, which are classified as non-peptidase homologues either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity.
    
 0.984
AARI_19890
Rieske (2Fe-2S) domain-containing protein; Match to protein domain PF00355.
  
 0.974
atpB
H(+)-transporting two-sector ATPase, chain A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
   
  
 0.934
AARI_21270
Conserved hypothetical membrane protein; Signal peptide predicted by SignalP 3.0 HMM (probability: 1.000) with cleavage site probability 0.994 between position 28 and 29. Presence of transmembrane helices.
    
   0.864
Your Current Organism:
Glutamicibacter arilaitensis
NCBI taxonomy Id: 861360
Other names: Arthrobacter arilaitensis CIP 108037, Arthrobacter arilaitensis Re117, G. arilaitensis Re117, Glutamicibacter arilaitensis Re117
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