EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   3.4.22.71 | 2 amylase-binding adhesin AbpA |
- |
Streptococcus parasanguinis |
(amylase-binding adhesin AbpA)2 + H2O |
- |
? |
| 3.4.22.71 | 2 amylase-binding adhesin AbpA |
- |
Streptococcus parasanguinis FW213 |
(amylase-binding adhesin AbpA)2 + H2O |
- |
? |
| 3.4.22.71 | Abz-KDFEVPTGVAM-Dap(Dnp)-NH2 + H2O |
- |
Streptococcus pyogenes |
? |
- |
? |
| 3.4.22.71 | Abz-KDFEVPTGVAM-Dap(Dnp)-NH2 + H2O |
- |
Streptococcus pyogenes M1 SF370 |
? |
- |
? |
| 3.4.22.71 | DNPNTGDE + H2O |
- |
Bacillus anthracis |
? |
- |
? |
| 3.4.22.71 | IsdC + H2O |
the enzyme cleaves the C-terminal sorting signal of IsdC at the NPQTN motif and rethers the polypeptide to the pentaglycine cell wall cross-bridge. During catalysis, the active site cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges |
Staphylococcus aureus |
? |
- |
? |
| 3.4.22.71 | IsdC + H2O |
the enzyme anchors the IsdC precursor with a C-terminal NPQTN motif sorting sognal, to the cell wall envelope. The sorting signal of IsdC is cleaved between threonine and asparagine of the NPQTN motif, and the carboxyl group of the thrteonine is amide-linked to the amino group of pentaglycine cross-bridges |
Staphylococcus aureus |
? |
- |
? |
| 3.4.22.71 | IsdC + H2O |
IsdC is a surface protein necessary for heme iron uptake in Bacillus anthracis. SrtB recognizes the NPKTG sequence present |
Bacillus anthracis |
? |
- |
? |
| 3.4.22.71 | Lmo2185 + H2O |
- |
Listeria monocytogenes |
? |
- |
? |
| 3.4.22.71 | Lmo2186 + H2O |
NPKSS is a sorting motif of Lmo2186. Recognition of NPKSS by SrtB, even when placed in the context of the heterologous sorting signal of Lmo2185. Proline at position 2, and not lysine at position 3, is essential for the recognition of NPKSS by SrtB |
Listeria monocytogenes |
? |
- |
? |
