Protein Family Models

This family of archaebacterial proteins, formerly known as DUF114, has been found to be a serine dehydrogenase proteinase distantly related to ClpP proteinases that belong to the serine proteinase superfamily. The family has a catalytic triad of Ser, Asp, His residues, which shows an altered residue ordering compared with the ClpP proteinases but similar to that of the carboxypeptidase clan [1]. [1]. 15752073. Identification and analysis of a new family of bacterial serine proteinases. Pandit SB, Srinivasan N;. In Silico Biol. 2004;4:563-572. (from Pfam)

Date:

2024-11-10

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

Members of this family may be found as free-standing proteins that are phage head maturation proteases, or as the N-terminal domain of phage fusion proteins that include a longer major capsid protein region.

Date:

2023-12-08

Clp protease ClpP is a serine protease, involved in several cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins

Date:

2024-10-17