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hslU protein (Maritimibacter alkaliphilus) - STRING interaction network
"hslU" - Unfoldase HslU in Maritimibacter alkaliphilus
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Predicted Interactions
gene neighborhood
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textmining
co-expression
protein homology
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hslUUnfoldase 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 (435 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 (183 aa)
  0.999
argS
Arginyl-tRNA synthetase (572 aa)
   
   
  0.833
dnaK
Heat shock protein 70 ; Acts as a chaperone (636 aa)
   
 
  0.831
dksA
RNA polymerase-binding transcription factor DksA ; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters (140 aa)
       
  0.824
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, [...] (382 aa)
 
 
  0.783
lon
ATP-dependent protease La ; 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 (801 aa)
   
 
  0.771
clpP
Endopeptidase Clp ; 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 (193 aa)
   
   
  0.770
groL
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (544 aa)
     
   
  0.764
groS
Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (86 aa)
     
   
  0.726
mutS
DNA mismatch repair protein MutS ; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (874 aa)
   
   
  0.722
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus, M. alkaliphilus HTCC2654, Maritimibacter, Maritimibacter Lee et al. 2007, Maritimibacter alkaliphilus, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus Lee et al. 2007, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
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