Protein Family Models

Members of this uncharacterized protein family, YfmH, and its paralog YfmF, share a conserved gene neighborhood with YfmI, which changes the side chain modification of elongation factor P Lys-32 from 5-aminopentanone to 5-aminopentanol, the functional form. Lineages with this particular form of EF-P modification included Bacillus, Staphylococcus, and Listeria. Both YfmF and YfmH belong to the M16 metalloprotease family. It is not clear yet if YfmF and YfmH represent missing components of the EF-P modification pathway that includes YfmI, or if the operon structure is widely conserved for some other reason. A solved crystal structure is available.

Gene:

yfmH

Date:

2024-08-05

Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp [1]. [1]. 11470436. Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Taylor AB, Smith BS, Kitada S, Kojima K, Miyaura H, Otwinowski Z, Ito A, Deisenhofer J;. Structure (Camb) 2001;9:615-625. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

M16 family metallopeptidase is a zinc-binding protein that may act as a peptidase cleaving small peptides close to a terminus, often including bonds on the amino side of basic residues such as arginine; similar to Escherichia coli zinc protease PqqL

Date:

2024-04-11