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
groES10 kD chaperonin (cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (91 aa)    
Predicted Functional Partners:
groEL
60 kD chaperonin (cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.999
dnaK
Heat shock protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.936
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- [...]
  
 
 0.920
htpG
Hsp90 family heat shock protein; Molecular chaperone. Has ATPase activity.
   
 
 0.850
hslU
Putative heat shock protein; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
   
  
 0.837
hslV
Putative ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.812
dnaJ
Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and [...]
   
 
 0.760
clpB
ATP-dependent CLP protease ATP-binding subunit; evidence=ISS; db_xref=cjejuni:Cj0509c; date=20070321; method=automatic:reciprocal fasta; Belongs to the ClpA/ClpB family.
  
 
 0.708
rnj
Putative metallo-beta-lactamase; An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
     
 0.702
clpA
ATP-dependent Clp protease ATP-binding subunit; evidence=ISS; db_xref=yenterocolitica:YE1518; date=20070321; method=automatic:reciprocal fasta; Belongs to the ClpA/ClpB family.
  
 
 0.688
Your Current Organism:
Helicobacter mustelae
NCBI taxonomy Id: 679897
Other names: H. mustelae 12198, Helicobacter mustelae 12198, Helicobacter mustelae str. 12198, Helicobacter mustelae strain 12198
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.