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clpP2 protein (Synechococcus elongatus PCC7942) - STRING interaction network
"clpP2" - ATP-dependent Clp protease proteolytic subunit 2 in Synechococcus elongatus PCC7942
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second shell of interactors
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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 proteolytic subunit 2; 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; Belongs to the peptidase S14 family (244 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 (449 aa)
 
  0.991
ABB58557.1
annotation not available (280 aa)
   
        0.838
ABB58558.1
annotation not available (228 aa)
   
        0.751
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; Belongs to the FKBP-type PPIase family. Tig subfamily (474 aa)
 
 
  0.733
ABB56292.1
annotation not available (824 aa)
     
 
  0.607
ABB58553.1
annotation not available (85 aa)
              0.595
clpB1
Chaperone protein ClpB 1; 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). Necessary for thermotolerance; Belongs [...] (883 aa)
     
 
  0.590
mopA
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (544 aa)
   
 
  0.586
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (953 aa)
     
   
  0.564
clpB2
Chaperone protein ClpB 2; 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) (895 aa)
     
 
  0.556
Your Current Organism:
Synechococcus elongatus PCC7942
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
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