STRINGSTRING
clpP protein (Sulfurovum sp. NBC371) - STRING interaction network
"clpP" - ATP-dependent Clp protease proteolytic subunit in Sulfurovum sp. NBC371
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
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
clpPATP-dependent Clp protease proteolytic subunit; 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 (195 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 (406 aa)
 
  0.990
def
Peptide 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 (174 aa)
 
   
  0.960
clpA
ATP-dependent Clp protease, ATP-binding subunit ClpA (729 aa)
   
 
  0.895
clpB
ATP-dependent Clp protease, ATP-binding subunit ClpB (857 aa)
   
 
  0.895
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 (427 aa)
   
 
  0.853
lon
ATP-dependent Lon protease; 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 (806 aa)
   
 
  0.841
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 (941 aa)
     
 
  0.828
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 [...] (657 aa)
     
 
  0.818
SUN_0542
ATP citrate synthase subunit 2 (606 aa)
 
 
  0.803
SUN_0014
Mg chelatase-like protein (527 aa)
   
        0.742
Your Current Organism:
Sulfurovum sp. NBC371
NCBI taxonomy Id: 387093
Other names: S. sp. NBC37-1, Sulfurovum, Sulfurovum Inagaki et al. 2004, Sulfurovum NBC37_1, Sulfurovum sp. NBC37-1, Sulfurovum sp. NBC371
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