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YSIRK-type signal peptide-containing protein
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)
glycoside hydrolase family 68 protein
This Pfam family consists of the glycosyl hydrolase 68 family, including several bacterial levansucrase enzymes, and invertase from zymomonas. [1]. 9726857. Cloning, nucleotide sequence, and expression in Escherichia coli. of levansucrase genes from the plant pathogens Pseudomonas. syringae pv. glycinea and P. syringae pv. phaseolicola.. Hettwer U, Jaeckel FR, Boch J, Meyer M, Rudolph K, Ullrich MS;. Appl Environ Microbiol 1998;64:3180-3187. (from Pfam)
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.
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