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
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (610 aa)    
Predicted Functional Partners:
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 [...]
 0.999
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- [...]
 
 0.999
SRA_02271
Glucan-binding protein C.
  
 0.987
groEL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.968
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 
 0.961
SRA_09733
Putative nitrogen fixation-like protein, NifU; COG0822 NifU homolog involved in Fe-S cluster formation.
 
 
 0.933
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.
  
  
 0.932
groES
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.927
SRA_04756
Putative Clp-like ATP-dependent protease, ATP-binding subunit; COG0542 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.841
SRA_06261
Putative Clp proteinase, ATP-binding subunit ClpB; COG0542 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.834
Your Current Organism:
Streptococcus ratti
NCBI taxonomy Id: 699248
Other names: S. ratti FA-1 = DSM 20564, Streptococcus ratti DSM 20564, Streptococcus ratti DSM 20564 = FA-1, Streptococcus ratti FA-1, Streptococcus ratti FA-1 = DSM 20564
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