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
groSChaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (110 aa)    
Predicted Functional Partners:
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 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 [...]
  
 
 0.963
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.942
EDR45946.1
Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98.
   
 
 0.874
clpP
ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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.
 
 
 0.863
EDR46654.1
Hypothetical protein; Psort location: Cytoplasmic, score: 8.87.
  
 
 0.834
EDR46849.1
Hypothetical protein; Psort location: Cytoplasmic, score: 8.87.
  
 
 0.834
rplL
Ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
  
  
 0.744
EDR45624.1
Putative chaperone protein DnaJ; KEGG: cme:CMJ043C 7.6e-09 phycocyanobilin lyase alpha subunit K02288; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 9.65.
 
 
 0.723
EDR48410.1
ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family.
  
 
 0.705
Your Current Organism:
Dorea formicigenerans
NCBI taxonomy Id: 411461
Other names: D. formicigenerans ATCC 27755, Dorea formicigenerans ATCC 27755
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