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]
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grpEHeat-shock protein (activation of DnaK); 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. Severa [...] (174 aa)    
Predicted Functional Partners:
dnaK
Class I heat-shock protein (molecular chaperone); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
hrcA
Heat inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.986
dnaJ
dnaJ protein, Heat-shock protein (activation of DnaK); 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-depende [...]
 
 
 0.978
groEL
CH60_SMI 60 kDa chaperonin (protein Cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.950
smi_1730
HSP70 family protein; Chaperone, homology to DnaK, COG0443; Belongs to the heat shock protein 70 family.
 
 0.941
groES
CH10_SMI 10 kDa chaperonin (protein Cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.938
ctsR
Pfam05848, firmicute transcriptional repressor of class III stress genes (CtsR); Belongs to the CtsR family.
   
  
 0.692
clpP
ATP-dependent CLP protease proteolytic subunit; 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.
   
 
 0.666
htpX
Heat shock protein, protease HtpX; COG0501, Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family.
  
  
 0.651
clpL
ATP-dependent Clp protease, ATP-binding subunit; COG0542; Belongs to the ClpA/ClpB family.
  
 
 0.642
Your Current Organism:
Streptococcus mitis
NCBI taxonomy Id: 365659
Other names: S. mitis B6, Streptococcus mitis B6, Streptococcus mitis str. B6, Streptococcus mitis strain B6
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