Protein Family Models

This domain is found in a wide variety of extracellular bacterial proteins often in multiple tandem copies. (from Pfam)

Date:

2024-08-14

Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus. (from Pfam)

Date:

2024-08-14

The [YF]SIRKxxxGxxS type of signal peptide appears at the start of many proteins of Streptococcus, Staphylococcus, and Enterococcus, but not in other lineages such as Bacillus. Recent work in Staphylococcus aureus has shown that septal secretion (targeting to the crosswall in dividing cells) of the YSIRK-containing staphylococcal protein A depends on SecA, SecDF, and the lipoteichoic acid synthase LtaS, all of which co-purify when the motif is modified to YSIRKxxxGxxL to block processing.

Date:

2024-12-19

This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.

Date:

2020-10-26