STRINGSTRING
clpX protein (Gloeobacter violaceus) - STRING interaction network
"clpX" - ATP-dependent protease ATP-binding subunit ClpX in Gloeobacter violaceus
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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
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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clpXATP-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)    
Predicted Functional Partners:
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)
 
  0.993
clpP2
ATP-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)
 
  0.992
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (419 aa)
 
 
 
  0.885
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 (461 aa)
   
   
  0.871
grpE
Heat shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- depe [...] (196 aa)
   
 
  0.852
glr2064
Endopeptidase Clp ATP-binding chain (819 aa)
   
 
  0.785
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)
   
 
  0.743
rps1
30S ribosomal protein S1 (320 aa)
 
     
  0.714
groL2
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (553 aa)
   
 
  0.701
groL1
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
   
 
  0.692
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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