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
groEL60 kD chaperonin (cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (545 aa)    
Predicted Functional Partners:
groES
10 kD chaperonin (cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 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- [...]
 
 0.998
dnaK
Heat shock protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.998
htpG
Hsp90 family heat shock protein; Molecular chaperone. Has ATPase activity.
   
 
 0.981
dnaJ
Chaperone 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, DnaK and [...]
 
 0.959
cbpA
Original (2000) note: Cj1229, cbpA, probable curved-DNA binding protein, len: 297 aa; similar to e.g. CBPA_ECOLI curved DNA-binding protein (306 aa), fatsa scores; opt: 514 z-score: 550.9 E(): 2.2e-23, 32.8% identity in 287 aa overlap. 52.0% identity to HP1024. Contains S00636 Nt-dnaJ domain signature, and Pfam match to entry PF00226 DnaJ, DnaJ domain; Updated (2006) note: Pfam domain PF01556 DnaJ C terminal region identified within CDS. Further support given to product function. Characterised in Escherichia coli with marginal identity score. Putative kept within product function. Func [...]
 
 0.937
hrcA
Putative heat shock regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.881
atpD
ATP synthase F1 sector beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family.
  
 0.872
hslU
ATP-dependent Hsl protease ATP-binding subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.871
hslV
ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
 
 0.871
Your Current Organism:
Campylobacter jejuni NCTC 11168
NCBI taxonomy Id: 192222
Other names: C. jejuni subsp. jejuni NCTC 11168 = ATCC 700819, Campylobacter jejuni subsp. jejuni ATCC 700819, Campylobacter jejuni subsp. jejuni ATCC 700819 = NCTC 11168, Campylobacter jejuni subsp. jejuni NCTC 11168, Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
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