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ATP-dependent Clp protease proteolytic subunit
The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion. [1]. 9390554. The structure of ClpP at 2.3 angstroms resolution suggests a. model for ATP-dependent proteolysis.. Wang J, Hartling JA, Flanagan JM;. Cell 1997;91:447-456. (from Pfam)
ATP-dependent Clp protease proteolytic subunit is a serine protease that catalyzes the hydrolysis of proteins to small peptides in the presence of ATP and Mg2+
Hydrolyzes proteins to small peptides; with the ATPase subunits ClpA or ClpX, ClpP degrades specific substrates
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