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groES protein (Xanthomonas campestris campestris) - STRING interaction network
"groES" - 10 kDa chaperonin in Xanthomonas campestris campestris
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
groES10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)    
Predicted Functional Partners:
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (546 aa)
 
 
  0.999
grpE
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- dependent [...] (197 aa)
   
   
  0.963
dnaK
Chaperone protein DnaK; Acts as a chaperone (642 aa)
 
 
  0.938
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (634 aa)
     
 
  0.905
clpB
Chaperone protein 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family (861 aa)
 
 
  0.905
clpP
ATP-dependent Clp protease proteolytic subunit; 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 (208 aa)
 
 
  0.881
rplL
50S 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 (121 aa)
   
   
  0.859
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (428 aa)
 
 
  0.855
XCC1667
Cytochrome c2 (131 aa)
   
   
  0.853
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5’-end of 16S ribosomal RNA (89 aa)
     
   
  0.842
Your Current Organism:
Xanthomonas campestris campestris
NCBI taxonomy Id: 340
Other names: X. campestris pv. campestris, Xanthomonas campestris, Xanthomonas campestris (pv. campestris), Xanthomonas campestris campestris, Xanthomonas campestris pv. campestris
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