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Mettu_0640 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_0640" - ATP-dependent Clp protease, ATP-binding subunit clpA in Methylobacter tundripaludum
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Mettu_0640ATP-dependent Clp protease, ATP-binding subunit clpA (757 aa)    
Predicted Functional Partners:
clpS
ATP-dependent Clp protease adapter protein ClpS ; Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (107 aa)
 
 
  0.999
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)
   
  0.984
dnaK
Heat shock protein 70 ; Acts as a chaperone (644 aa)
   
 
  0.975
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)
   
 
  0.974
grpE
HSP-70 cofactor ; 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- depend [...] (203 aa)
   
 
  0.968
Mettu_3601
Heat shock protein 70 (432 aa)
   
 
  0.920
Mettu_3235
DnaK-related protein (646 aa)
   
 
  0.920
Mettu_0186
Putative chaperone heat-shock protein (932 aa)
   
 
  0.920
htpG
High temperature protein G ; Molecular chaperone. Has ATPase activity (642 aa)
   
 
  0.884
Mettu_3874
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 (424 aa)
   
 
  0.877
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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