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clpP2 protein (Gloeobacter violaceus) - STRING interaction network
"clpP2" - ATP-dependent Clp protease-like protein in Gloeobacter violaceus
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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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clpP2ATP-dependent Clp protease-like protein; 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 (218 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 (437 aa)
 
  0.992
glr2064
Endopeptidase Clp ATP-binding chain (819 aa)
   
 
  0.877
clpB
Endopeptidase Clp ATP-binding chain B; 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)
   
 
  0.877
clpP1
ATP-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 (197 aa)
 
     
0.829
def2
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 (187 aa)
 
   
  0.773
groL1
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
 
 
  0.766
gll3765
Hypothetical protein (236 aa)
              0.763
groL2
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (553 aa)
 
 
  0.741
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity (614 aa)
     
   
  0.739
glr1542
Endopeptidase Clp ATP-binding chain (778 aa)
 
 
  0.734
Your Current Organism:
Gloeobacter violaceus
NCBI taxonomy Id: 251221
Other names: G. violaceus, G. violaceus PCC 7421, Gloeobacter, Gloeobacter violaceus, Gloeobacter violaceus ATCC 29082, Gloeobacter violaceus PCC 7421, Gloeobacter violaceus str. PCC 7421, Gloeobacter violaceus strain PCC 7421, Gloeobacterales, Gloeobacterales Cavalier-Smith 2002, Gloeobacteria, Gloeobacteria Cavalier-Smith 2002
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