STRINGSTRING
clpP protein (Prevotella amnii) - STRING interaction network
"clpP" - Endopeptidase Clp in Prevotella amnii
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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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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 (221 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 (410 aa)
  0.999
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 (863 aa)
   
 
  0.887
HMPREF9018_0883
ATPase family associated with various cellular activities (AAA) (871 aa)
   
 
  0.887
HMPREF9018_2057
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 (944 aa)
     
 
  0.852
HMPREF9018_1979
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 (977 aa)
     
 
  0.852
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 [...] (681 aa)
     
 
  0.847
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 (811 aa)
   
 
  0.800
tig
Trigger factor (455 aa)
   
 
  0.757
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 (186 aa)
 
   
  0.710
recQ
ATP-dependent DNA helicase RecQ (727 aa)
   
      0.636
Your Current Organism:
Prevotella amnii
NCBI taxonomy Id: 679191
Other names: P. amnii, P. amnii CRIS 21A-A, Prevotella amnii, Prevotella amnii CRIS 21A-A, Prevotella amnii Lawson et al. 2008, Prevotella amnii str. CRIS 21A-A, Prevotella amnii strain CRIS 21A-A
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