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
BF49_3428Transcriptional regulator PhnF. (243 aa)    
Predicted Functional Partners:
BF49_3427
PhnG protein.
 
  
 0.981
BF49_3424
PhnJ protein; Catalyzes the breakage of the C-P bond in alpha-D-ribose 1- methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose. Belongs to the PhnJ family.
 
  
 0.980
BF49_3425
PhnI protein.
 
  
 0.979
BF49_3426
PhnH protein.
 
  
 0.977
BF49_3423
Phosphonates transport ATPbinding protein PhnK.
 
  
 0.971
BF49_3422
Phosphonates transport ATPbinding protein PhnL.
 
  
 0.970
BF49_3421
Metaldependent hydrolase involved in phosphonate metabolism.
 
  
 0.955
BF49_3431
Phosphonate ABC transporter phosphatebinding periplasmic component TC 3A191.
 
  
 0.925
BF49_3434
Metaldependent hydrolase involved in phosphonate metabolism.
 
  
 0.918
phnN
ATPbinding protein PhnN Guanylate kinase EC 2748; Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
 
  
 0.914
Your Current Organism:
Bradyrhizobium sp.
NCBI taxonomy Id: 376
Other names: B. sp.
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