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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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grpEPutative 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-de [...] (179 aa)    
Predicted Functional Partners:
dnaK
Putative chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
hrcA
Putative Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.992
dnaJ
Putative chaperone protein 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 betwee [...]
 
 
 0.992
groL
Putative chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.989
groES
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.984
clpP
ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
   
 
 0.835
polA
Putative DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
  
 0.789
msrA
Peptide methionine sulfoxide reductase MsrA/msrB family protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
   
 
 0.768
ctsR
Transcriptional regulator CtsR; Belongs to the CtsR family.
   
  
 0.721
EHI73893.1
Hypothetical protein; Belongs to the ClpA/ClpB family.
  
 
 0.715
Your Current Organism:
Streptococcus criceti
NCBI taxonomy Id: 873449
Other names: S. criceti HS-6, Streptococcus criceti HS-6, Streptococcus criceti str. HS-6, Streptococcus criceti strain HS-6
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