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clpP protein (Methylobacillus flagellatus) - STRING interaction network
"clpP" - ATP-dependent Clp protease proteolytic subunit ClpP in Methylobacillus flagellatus
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
clpPATP-dependent Clp protease proteolytic subunit ClpP; 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 (213 aa)    
Predicted Functional Partners:
clpX
ATP-dependent 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 (421 aa)
 
  0.998
tig
Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (434 aa)
 
 
  0.947
clpB
ATPase AAA-2; 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 (861 aa)
     
 
  0.921
lon
Lon-A peptidase; 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 (811 aa)
   
 
  0.920
Mfla_0508
ATPase AAA-2 (763 aa)
     
 
  0.869
Mfla_1170
ATPase AAA-2 (949 aa)
     
 
  0.805
uvrA
Excinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (939 aa)
     
 
  0.769
uvrB
Excinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] (679 aa)
       
 
  0.766
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (544 aa)
   
 
  0.743
Mfla_1168
FtsH-2 peptidase; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (605 aa)
     
   
  0.730
Your Current Organism:
Methylobacillus flagellatus
NCBI taxonomy Id: 265072
Other names: M. flagellatus, M. flagellatus KT, Methylobacillus, Methylobacillus flagellatus, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT
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