EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.17 | Staphylococcus aureus | - |
- |
- |
2.3.2.18 | Staphylococcus aureus | - |
- |
- |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.2.17 | physiological function | femA mutants leading to truncated proteins still produce intact FemB while exhibiting a phenotype identical to femAB double mutants, such as same muropeptide pattern. FemA is essential for the addition of glycine residues 2 and 3 only to the staphylococcal interpeptide bridge | Staphylococcus aureus |
2.3.2.18 | physiological function | FemB is involved in the addition of exclusively glycine residues 4 and 5 to the staphylococcal interpeptide bridge. femA mutants leading to truncated proteins still produce intact FemB while exhibiting a phenotype identical to femAB double mutants, such as same muropeptide pattern. FemA is essential for the addition of glycine residues 2 and 3 only to the staphylococcal interpeptide bridge, and FemB cannot substitute for FemA | Staphylococcus aureus |