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	ATP	only ATP and dATP support alpha-casein degradation	29858	
3.4.21.92	ATP	proteolytic activity	29860	
3.4.21.92	dATP	only ATP and dATP support alpha-casein degradation	29858	
3.4.21.92	dATP	proteolytic activity	29860	
3.4.21.92	additional information	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	additional information	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