Protein Family Models

Date:

2024-08-14

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

S49 family peptidase similar to SppA (Signal peptide peptidase A), which is a membrane-bound serine protease that functions to cleave remnant signal peptides in the membrane left behind by the action of signal peptidases

Date:

2023-01-10

The related but duplicated, double-length protein SppA (protease IV) of E. coli was shown experimentally to degrade signal peptides as are released by protein processing and secretion. This protein shows stronger homology to the C-terminal region of SppA than to the N-terminal domain or to the related putative protease SuhB. The member of this family from Bacillus subtilis was shown to have properties consistent with a role in degrading signal peptides after cleavage from precursor proteins, although it was not demonstrated conclusively.

Gene:

sppA

Date:

2021-05-12