EC Number   |
Cofactor |
Reference |
|---|
   3.4.21.92 | ATP |
- |
710200, 734574 |
| 3.4.21.92 | ATP |
ATP dependent, for full proteolytic activity ClpP must associate with one of two related ATPase subunits, ClpA or ClpX, other nucleoside triphosphates cannot substitute for ATP |
653260 |
| 3.4.21.92 | 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 |
29867 |
| 3.4.21.92 | ATP |
ATP hydrolysis is required for protein breakdown but not for hydrolysis of small peptides |
29864 |
| 3.4.21.92 | ATP |
cleavage of peptides of more than five amino acids residues by ClpP requires activation by ClpA and either ATP or a nonhydrolyzable analog of ATP such as ATPgammaS or 5'-adenylyl imidodiphosphate |
29858 |
| 3.4.21.92 | ATP |
composed of the proteolytic subunit ClpP and the regulatory ATPase |
653568 |
| 3.4.21.92 | more |
degradation of GFP-K17 is MecA dependent and prevented in the presence of ComS, MecA and ComS can be degraded by ClpCP. ComS competes with ComK for MecA binding and protects MecA from degradation by ClpP. The degradation of ComS requires the presence of MecA, which acts as an adapter for both ComS and ComK. MecA knockout strain fails to target ComK for degradation by ClpCP |
683866 |
| 3.4.21.92 | more |
MecA facilitates ClpC oligomerization into a complex containing both ClpC and MecA. Formation of this complex is a prerequisite for all ClpC mediated activities, including ATPase activity, substrate recognition and interaction with ClpP |
683899 |
| 3.4.21.92 | ATP |
only ATP and dATP support alpha-casein degradation |
29858 |
| 3.4.21.92 | dATP |
only ATP and dATP support alpha-casein degradation |
29858 |
