EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   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 |
Bacillus anthracis |
? |
- |
? |
| 3.4.22.B63 | BasH polypeptide + H2O |
sortase C specifically recognizes and cleaves the BasI 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 |
Bacillus anthracis |
? |
- |
? |
| 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 |
Bacillus anthracis |
? |
- |
? |
| 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 |
Bacillus anthracis |
? |
- |
? |
| 3.4.22.B63 | BasI polypeptide + H2O |
sortase C specifically recognizes and cleaves the BasI 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 |
Bacillus anthracis |
? |
- |
? |
| 3.4.22.B63 | BasI polypeptide + H2O |
the LPNTA motif of BasI polypeptide 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 |
Bacillus anthracis |
? |
- |
? |
| 3.4.22.B63 | Dabcyl-ancillary protein 1-Edans + H2O |
preferred substrate of SrtC2 |
Streptococcus agalactiae serogroup V |
? |
- |
? |
| 3.4.22.B63 | Dabcyl-ancillary protein 1-Edans + H2O |
preferred substrate of SrtC2 |
Streptococcus agalactiae serogroup V ATCC BAA-611 |
? |
- |
? |
| 3.4.22.B63 | Dabcyl-ancillary protein 2-Edans + H2O |
preferred substrate of SrtC1 |
Streptococcus agalactiae serogroup V |
? |
- |
? |
| 3.4.22.B63 | Dabcyl-ancillary protein 2-Edans + H2O |
preferred substrate of SrtC1 |
Streptococcus agalactiae serogroup V ATCC BAA-611 |
? |
- |
? |
