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Results 1 - 10 of 11 > >>
EC Number
Cofactor
Commentary
Reference
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
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
ATP
ATP hydrolysis is required for protein breakdown but not for hydrolysis of small peptides
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; only ATP and dATP support alpha-casein degradation
ATP
composed of the proteolytic subunit ClpP and the regulatory ATPase
ATP
proteolytic activity
dATP
only ATP and dATP support alpha-casein degradation
dATP
proteolytic activity
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
Results 1 - 10 of 11 > >>