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