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hslU protein (Methylobacter tundripaludum) - STRING interaction network
"hslU" - Unfoldase HslU in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
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 (439 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 (182 aa)
  0.999
htpG
High temperature protein G ; Molecular chaperone. Has ATPase activity (642 aa)
     
   
  0.918
dnaK
Heat shock protein 70 ; Acts as a chaperone (644 aa)
     
   
  0.915
groS
Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)
     
   
  0.888
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. Also required for regulation of fis expression (144 aa)
       
  0.864
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, [...] (376 aa)
     
 
  0.853
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 (858 aa)
     
   
  0.838
groL
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (550 aa)
     
   
  0.836
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 (215 aa)
   
   
  0.820
argS
Arginyl-tRNA synthetase (586 aa)
   
   
  0.812
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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