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
betACholine dehydrogenase; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. (567 aa)    
Predicted Functional Partners:
betB
Betaine-aldehyde dehydrogenase; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid.
 
 
 0.974
ARQ74607.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.940
betI
Transcriptional regulator BetI; Repressor involved in choline regulation of the bet genes.
 
  
 0.823
psd
Phosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
     
  0.800
ARQ74799.1
Cellulose synthase regulator BcsB; Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP); Belongs to the AcsB/BcsB family.
  
 
 0.507
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).
  
 
 0.451
ARQ73348.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.448
ARQ74488.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.448
ARQ75294.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.448
ccoP
Cytochrome c oxidase, cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 
 0.434
Your Current Organism:
Pseudomonas fragi
NCBI taxonomy Id: 296
Other names: ATCC 4973, Bacterium fragi, CCUG 556, CFBP 4556, CIP 55.4, DSM 3456, HAMBI 28, IFO 3458, LMG 2191, LMG:2191, NBRC 3458, NCCB 69033, NCIB 8542, NCIB:8542, NCTC 10689, NRRL B-25, NRRL B-727, NRRL:B:25, P. fragi, Pseudomonas fragariae, VKM B-898, VKM:B:898
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