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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
groLChaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (539 aa)    
Predicted Functional Partners:
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
grpE
Co-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 [...]
 
 0.985
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 [...]
 
 0.969
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.968
DnaK2
DnaK family protein; KEGG: ctx:Clo1313_0933 3.1e-63 chaperone protein DnaK K04043; Psort location: Cytoplasmic, score: 9.97.
 
 0.933
KXU57535.1
DnaK family protein; KEGG: ctu:CTU_25580 3.9e-79 hscC; chaperone protein hscC K04045; Psort location: Cytoplasmic, score: 9.97.
 
 0.916
FtsH
ATP-dependent metallopeptidase HflB; KEGG: ssr:SALIVB_0013 0. ftsH; cell division protein K03798; Psort location: CytoplasmicMembrane, score: 10.00.
   
 0.884
KXU57926.1
KEGG: ste:STER_0545 6.7e-123 peptidyl-prolyl cis-trans isomerase; K03767 peptidyl-prolyl cis-trans isomerase A (cyclophilin A); Psort location: Periplasmic, score: 9.44.
 
 0.862
KXU57534.1
DnaJ domain protein.
   
 0.862
KXU58500.1
Hypothetical protein; KEGG: stj:SALIVA_1154 6.7e-100 signal transduction histidine kinase LytS; Psort location: CytoplasmicMembrane, score: 10.00.
  
 0.841
Your Current Organism:
Streptococcus salivarius
NCBI taxonomy Id: 1304
Other names: ATCC 7073, CCUG 11878, CCUG 17825, CCUG 50207, CIP 102503, DSM 20560, JCM 5707, LMG 11489, LMG:11489, NCIMB 701779, NCTC 8618, S. salivarius, Streptococcus salivarius subsp. salivarius, Streptococcus sp. FStet12, Streptococcus sp. HSISS4
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