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clpX protein (Acidaminococcus intestini) - STRING interaction network
"clpX" - ATP-dependent Clp protease in Acidaminococcus intestini
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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 Clp protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (425 aa)    
Predicted Functional Partners:
clpP
ATP-dependent Clp 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 (199 aa)
  0.999
lon
ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (776 aa)
   
 
  0.975
Acin_1917
ATP-dependent Clp protease, proteolytic subunit ClpP (244 aa)
 
  0.968
Acin_1344
Hypothetical protein (227 aa)
 
  0.965
Acin_1975
Hypothetical protein (226 aa)
 
  0.965
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 (375 aa)
     
 
  0.918
tig
Cell division 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 (439 aa)
   
   
  0.914
groL
Chaperonin groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
 
 
  0.903
grpE
Hypothetical 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- de [...] (193 aa)
   
 
  0.813
engB
GTP-binding protein; Necessary for normal cell division and for the maintenance of normal septation (210 aa)
         
  0.813
Your Current Organism:
Acidaminococcus intestini
NCBI taxonomy Id: 568816
Other names: A. intestini, A. intestini RyC-MR95, Acidaminococcus intestini, Acidaminococcus intestini Jumas-Bilak et al. 2007, Acidaminococcus intestini RyC-MR95, Acidaminococcus intestini strain RyC-MR95, Acidaminococcus sp. ADV 255.99
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