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Literature summary for 3.4.21.92 extracted from

  • Maurizi, M.R.
    ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli (1991), Biochem. Soc. Trans., 19, 719-723.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
700000
-
E. coli, complex of subunits ClpA with ClpP in presence of ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Subunits

Subunits Comment Organism
More ClpP subunits (MW 21500 Da) are arranged in two hexagonal rings directly superimposed on each other, ClpA (subunit 83000) and ClpP do not associate in absence of ATP Escherichia coli
More ClpA subunit has ATPase activity, ClpP subunit has the proteolytic active site and is activated by ClpA in the presence of ATP Escherichia coli
More ClpA bound with ATP associates with ClpP to form an active proteolytic complex with MW 700000 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP ATP has two functions in activating Clp protease: an allosteric role in promoting association between the subunits and a mechanistically undefined role in promoting continuous rounds of peptide bond cleavage. The functions may be separately fulfilled by the two ATP-binding sites identified by sequence analysis on each ClpA subunit Escherichia coli