Protein Family Models

This family of proteins are functionally uncharacterised. This protein is found in bacteria. Proteins in this family are typically between 564 to 612 amino acids in length. (from Pfam)

Date:

2024-08-14

This homology domain, GlyGly-CTERM, shares a species distribution with rhombosortase (TIGR03902), a subfamily of rhomboid-like intramembrane serine proteases. It is recognized, and cleaved, by rhombosortase. Shewanella species have the largest number of target proteins per genome, up to thirteen. The domain occurs at the extreme carboxyl-terminus of a diverse set of proteins, most of which are enzymes with conventional signal sequences and with hydrolytic activities: nucleases, proteases, agarases, etc. The agarase AgaA from Vibro sp. strain JT0107 is secreted into the medium, while the same protein heterologously expressed in E. coli is retained in the cell fraction. VesB, from Vibrio cholerae, was shown to be processed by rhombosortase so as to expose the second Gly of the motif, and then to be linked to a glycerophosphoethanolamine, prior to type II secretion. Note that both the processing, and the chemical structure of the domain (motif, hydrophobic predicted transmembrane helix, cluster of basic residues), closely parallels those of the LPXTG/sortase system, the PGF-CTERM/archaseosortase system, and the PEP-CTERM/exosortase(EpsH) system.

Date:

2023-07-12