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
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
grpEHeat 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- [...] (209 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.998
GAN54220.1
Chaperone protein dnaK.
  
 0.992
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.987
dnaJ
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 between DnaJ, D [...]
 
 
 0.976
groS
Heat shock protein GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.968
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.
  
  
 0.962
GAN53725.1
ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
   
  
 0.942
hslV
ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.929
GAN52875.1
Chaperone protein DnaJ.
 
 
 0.927
lon
ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
  
 0.886
Your Current Organism:
Tanticharoenia sakaeratensis
NCBI taxonomy Id: 1231623
Other names: T. sakaeratensis NBRC 103193, Tanticharoenia sakaeratensis BCC 15772, Tanticharoenia sakaeratensis NBRC 103193
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