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clpP1 protein (Synechocystis sp. PCC6803) - STRING interaction network
"clpP1" - ATP-dependent protease in Synechocystis sp. PCC6803
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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
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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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clpP1ATP-dependent protease; 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 (198 aa)    
Predicted Functional Partners:
clpX
ATP-dependent protease ATPase subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (445 aa)
 
  0.998
clpB1
ClpB protein; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity) (898 aa)
   
 
  0.968
clpB2
ClpB protein; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity) (872 aa)
   
 
  0.968
clpC
ATP-dependent Clp protease regulatory subunit (821 aa)
   
 
  0.967
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 (By similarity) (471 aa)
   
 
  0.894
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 (970 aa)
     
 
  0.887
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 [...] (669 aa)
     
 
  0.885
groS
10kD co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (106 aa)
   
   
  0.874
groL1
60kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (541 aa)
   
 
  0.860
dnaK1
DnaK protein; Acts as a chaperone (692 aa)
   
   
  0.852
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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