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clpP1 protein (Synechococcus elongatus PCC7942) - STRING interaction network
"clpP1" - ATP-dependent Clp protease proteolytic subunit 1 in Synechococcus elongatus PCC7942
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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clpP1ATP-dependent Clp protease proteolytic subunit 1; 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 (197 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)
 
  0.957
tuf
Elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (409 aa)
     
   
  0.636
thf1
Protein Thf1; May be involved in photosynthetic membrane biogenesis (280 aa)
   
        0.620
ABB56292.1
annotation not available (824 aa)
     
 
  0.607
mopA
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (544 aa)
   
 
  0.593
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
ABB56717.1
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (555 aa)
   
 
  0.564
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
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 (192 aa)
 
   
  0.518
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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