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 GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)    
Predicted Functional Partners:
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.998
ADW17097.1
GrpE protein; COGs: COG0576 Molecular chaperone GrpE (heat shock protein); InterPro IPR000740; KEGG: dak:DaAHT2_0057 GrpE protein; PFAM: GrpE protein; SPTR: Protein grpE; PFAM: GrpE.
 
 0.993
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 
 0.968
hslU
Heat shock protein HslVU, ATPase subunit HslU; 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.
   
  
 0.955
ADW18122.1
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR003095: IPR012724: IPR018253: IPR001623: IPR 001305: IPR002939; KEGG: dps:DP1482 chaperone protein DnaJ; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; DnaJ central domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Chaperone protein dnaJ; TIGRFAM: chaperone protein DnaJ; PFAM: DnaJ domain; DnaJ central domain (4 repeats); DnaJ C terminal region; TIGRFAM: chaperone protein DnaJ.
 
 0.948
ADW17196.1
KEGG: tau:Tola_0702 hypothetical protein; SPTR: Putative uncharacterized protein.
   
 
 0.918
ADW18515.1
Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623: IPR003095: IPR002939: IPR018253; KEGG: dps:DP1965 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Related to chaperone protein DnaJ; PFAM: DnaJ C terminal region; DnaJ domain; TIGRFAM: chaperone protein DnaJ.
 
 0.912
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.903
ADW17221.1
Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: dps:DP2937 heat shock protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Related to heat shock protein DnaJ; PFAM: DnaJ domain; Tellurite resistance protein TerB.
  
 0.892
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.