STRINGSTRING
clpP protein (Pedobacter sp. BAL39) - STRING interaction network
"clpP" - Endopeptidase Clp in Pedobacter sp. BAL39
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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[Homology]
Score
clpPEndopeptidase 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 (233 aa)    
Predicted Functional Partners:
clpX
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 (392 aa)
  0.995
def
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (184 aa)
 
   
  0.851
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 (865 aa)
   
 
  0.778
PBAL39_06346
ATP-dependent Clp protease, ATP-binding subunit (844 aa)
   
 
  0.778
groL
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (546 aa)
 
 
  0.777
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 (825 aa)
   
 
  0.760
PBAL39_14094
Putative ATP-dependent protease (828 aa)
   
 
  0.723
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 [...] (678 aa)
       
 
  0.714
PBAL39_20720
FKBP-type peptidyl-prolyl cis-transisomerase (Trigger factor) (448 aa)
   
 
  0.708
PBAL39_24033
UvrABC system protein 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 (937 aa)
     
 
  0.706
Your Current Organism:
Pedobacter sp. BAL39
NCBI taxonomy Id: 391596
Other names: P. sp. BAL39, Pedobacter BAL39, Pedobacter sp. BAL39
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