EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.24.29 | extracellular | the enzyme is secreted | Staphylococcus aureus | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.29 | additional information | metalloprotease | Staphylococcus aureus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.29 | Bap + H2O | Staphylococcus aureus | a surface-anchored protein | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.24.29 | Staphylococcus aureus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.29 | Bap + H2O | a surface-anchored protein | Staphylococcus aureus | ? | - |
? |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.24.29 | malfunction | the sigB mutant strain overexpresses the surface-anchored protein Bap, that is essential for biofilm formation in the model strain. Staphylococcus aureus completely inhibits the biofilm formation of the mutant strain via Aur and SspA, two proteases that are overexpressed in the sigB mutant strain and are capable of degrading Bap | Staphylococcus aureus |
3.4.24.29 | physiological function | extracellular proteases Aur and SspA inhibit protein-dependent biofilm formation by Staphylococcus aureus, detailed overview | Staphylococcus aureus |