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
KPL89654.1Cytochrome oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (195 aa)    
Predicted Functional Partners:
coxA-2
Cytochrome C oxidase; 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
coxB-2
Hypothetical protein; 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
coxA
Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family.
 
 0.997
coxA-3
Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.997
coxB
Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
coxB-3
Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
KPL87676.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
nuoH
NADH-quinone oxidoreductase; 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.
  
 
 0.989
atpB
Hypothetical protein; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
   
 
 0.989
nuoC-2
NADH dehydrogenase; 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 30 kDa subunit family. In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 
 0.987
Your Current Organism:
Ardenticatena maritima
NCBI taxonomy Id: 872965
Other names: A. maritima, ATCC BAA-2145, Ardenticatena maritima Kawaichi et al. 2013, DSM 23922, JCM 17282, KCTC 23289, NBRC 107679, filamentous thermophilic bacterium 110S, strain 110S
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