EC Number   |
Natural Substrates |
|---|
   3.4.22.B63 | BasH polypeptide + H2O |
sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine. Sortase C substrate BasH is expressed in the forespore |
| 3.4.22.B63 | BasI polypeptide + H2O |
sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine |
| 3.4.22.B63 | BasI polypeptide + H2O |
the LPNTA motif of BasI is cleaved between the threonine and the alanine residue. The C-terminal carboxyl group of threonine is subsequently amide linked to the side chain amino group of diaminopimelic acid within the wall peptides of Bacillus anthracis peptidoglycan (predivisional cell envelope). Sortase C with an active-site cysteine and the LPNTA sorting signal of BasI are required for anchoring of the polypeptide to the cell wall envelope |
| 3.4.22.B63 | Dabcyl-ancillary protein 1-Edans + H2O |
preferred substrate of SrtC2 |
| 3.4.22.B63 | Dabcyl-ancillary protein 2-Edans + H2O |
preferred substrate of SrtC1 |
| 3.4.22.B63 | Dabcyl-BP-1 peptide-Edans + H2O |
- |
| 3.4.22.B63 | more |
assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF |
| 3.4.22.B63 | more |
of the three genes for structural subunits, rrgB encodes the major pilin, while rrgA and rrgC encode ancillary pilin subunits decorating the pilus shaft and tip. Deletion of all three pilus associated sortase genes, srtB, srtC and srtD, completely prevents pilus biogenesis. Both SrtB and SrtC act as pilus subunit polymerases, with SrtB processing all three pilus subunit proteins, while SrtC processes only RrgB and RrgA |
| 3.4.22.B63 | more |
pilus-associated sortase C from Streptococcus pneumoniae acts as a polymerase for the pilus subunit proteins RrgA and RrgB |
| 3.4.22.B63 | more |
SrtC-1, SrtC-2, and SrtC-3 are responsible for RlrA pilus assembly and exhibit functional redundancy with respect to backbone assembly and cell wall localization. SrtC-3 is required for the incorporation of the accessory subunits RrgA and RrgC. Deleterious effect on pilus assembly upon alteration of the cell wall sorting signals of the accessory subunit proteins |
