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Literature summary extracted from
- Sortase enzymes in Gram-positive bacteria (2011), Mol. Microbiol., 82, 1044-1059.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.B64 | Bacillus cereus | - |
- |
- |
| 3.4.22.71 | Staphylococcus aureus | A0A0H3JPP1 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.22.B64 | SrtD | - |
Bacillus cereus |
| 3.4.22.71 | SrtB | - |
Staphylococcus aureus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.22.B64 | physiological function | sortase D links major pilin protein BcpA and minor tip pilin BcpB together. The enzyme cleaves related sorting signals within BcpA (LPVTG) and BcpB (IPNTG), and catalyses a transpeptidation that joins the threonine residues in each signal to the side-chain of Lys162 in BcpA (located within a pilin motif) | Bacillus cereus |
| 3.4.22.71 | physiological function | sortase attaches hemoproteins to the cell wall | Staphylococcus aureus |
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Release 2023.1 (January 2023)
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