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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
ctaBProtoheme 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. (312 aa)    
Predicted Functional Partners:
ctaG
Cytochrome C oxidase assembly protein; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I; Belongs to the COX11/CtaG family.
 
 0.998
ctaA
Heme A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 2 subfamily.
 
 0.998
ctaD
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.
 
 0.993
coxC
Cytochrome B562; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.992
coxB
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).
 
 
 0.990
KIU51968.1
Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family.
 
 0.981
KIU51969.1
Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.977
KIU51967.1
Cytochrome O ubiquinol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.965
KIU51970.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.941
KIU44651.1
Cytochrome C; 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.
 
 0.941
Your Current Organism:
Bradyrhizobium elkanii
NCBI taxonomy Id: 29448
Other names: ATCC 49852, B. elkanii, Bradyrhizobium sp. AK1, Bradyrhizobium sp. AK3, Bradyrhizobium sp. URO14, Bradyrhizobium sp. URO7, Bradyrhizobium sp. mas1, Bradyrhizobium sp. mas10, Bradyrhizobium sp. mas11, Bradyrhizobium sp. mas12, Bradyrhizobium sp. mas17, Bradyrhizobium sp. mas18, Bradyrhizobium sp. mas19, Bradyrhizobium sp. mas20, Bradyrhizobium sp. mas21, Bradyrhizobium sp. mas22, Bradyrhizobium sp. mas23, Bradyrhizobium sp. mas25, Bradyrhizobium sp. mas26, Bradyrhizobium sp. mas27, Bradyrhizobium sp. mas29, Bradyrhizobium sp. mas30, Bradyrhizobium sp. mas31, Bradyrhizobium sp. mas40, Bradyrhizobium sp. mas42, Bradyrhizobium sp. mas6, Bradyrhizobium sp. mas7, Bradyrhizobium sp. mas8, Bradyrhizobium sp. mas9, DSM 11554, IFO 14791, LMG 6134, LMG:6134, NBRC 14791, USDA 76
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