Protein Family Models

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)

Date:

2024-10-16

Hydrolyzes proteins to small peptides; with the ATPase subunits ClpA or ClpX, ClpP degrades specific substrates

Date:

2021-10-28

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+

Date:

2016-05-13

Date:

2021-11-22