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hslU protein (Yersinia pseudotuberculosis) - STRING interaction network
"hslU" - ATP-dependent protease ATPase subunit HslU in Yersinia pseudotuberculosis
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Known Interactions
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Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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hslUATP-dependent protease 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 (443 aa)    
Predicted Functional Partners:
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (174 aa)
 
  0.999
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (622 aa)
     
   
  0.942
dnaK
Chaperone protein DnaK; Acts as a chaperone (636 aa)
   
 
  0.936
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 [...] (379 aa)
     
 
  0.935
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; Belongs to the ClpA/ClpB family (857 aa)
     
   
  0.930
lon
Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (784 aa)
 
 
  0.922
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 [...] (192 aa)
     
   
  0.886
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (548 aa)
   
   
  0.879
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 (207 aa)
   
  0.841
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
     
   
  0.806
Your Current Organism:
Yersinia pseudotuberculosis
NCBI taxonomy Id: 633
Other names: ATCC 29833, Bacillus pseudotuberkulosis, Bacterium pseudotuberculosis, CCUG 5855, CIP 55.85, DSM 8992, NCTC 10275, Pasteurella pseudotuberculosis, Shigella pseudotuberculosis, Y. pseudotuberculosis, Yersinia pseudotuberculosis
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