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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[Homology]
Score
grpECo-chaperone 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-depend [...] (179 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
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 [...]
 
 
 0.990
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.990
hrcA
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.
  
  
 0.980
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.958
scrB
Sucrose-6-phosphate hydrolase; Enables the bacterium to metabolize sucrose as a sole carbon source; Belongs to the glycosyl hydrolase 32 family.
   
 
 0.718
clpC_1
Negative regulator of genetic competence ClpC/MecB; Identified by match to protein family HMM PF00004; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family.
  
 
 0.705
clpC_2
Negative regulator of genetic competence ClpC/MecB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02861; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family.
  
 
 0.705
clpC_3
Negative regulator of genetic competence ClpC/MecB; Identified by match to protein family HMM PF00004; match to protein family HMM PF02151; match to protein family HMM PF07724; match to protein family HMM PF07728; Belongs to the ClpA/ClpB family.
  
 
 0.705
clpP_1
ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Identified by match to protein family HMM PF00574.
   
 
 0.631
Your Current Organism:
Streptococcus porcinus
NCBI taxonomy Id: 873448
Other names: S. porcinus str. Jelinkova 176, Streptococcus porcinus str. Jelinkova 176, Streptococcus porcinus strain Jelinkova 176
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.