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.
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
cbpADNA-binding protein DnaJ. (310 aa)    
Predicted Functional Partners:
Ljam_0076
Putative chaperone-modulator protein CbpM.
 
 
 0.990
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.986
Ljam_0503
Polyketide synthase.
   
 
 0.916
Ljam_1060
Polyketide synthase.
   
 
 0.916
grpE
Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...]
 
 
 0.916
htpG
Class III heat-shock protein HtpG(molecular chaperone); Molecular chaperone. Has ATPase activity.
  
 0.856
arp_1
Ankyrin repeat protein.
    
 0.837
htpB
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.799
Ljam_0077
Phospholipid binding protein.
       0.730
groES
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.627
Your Current Organism:
Legionella jamestowniensis
NCBI taxonomy Id: 455
Other names: ATCC 35298, CCUG 29669, CIP 103845, DSM 19215, JCM 7590, L. jamestowniensis, Legionella jamestownensis, NCTC 11981, strain JA-26-G1-E2
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