EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.2.16 | additional information | in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wild-type strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins | Staphylococcus aureus |
2.3.2.17 | additional information | in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wildtype strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins | Staphylococcus aureus |
2.3.2.18 | additional information | in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wildtype strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins | Staphylococcus aureus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.16 | Staphylococcus aureus | - |
- |
- |
2.3.2.17 | Staphylococcus aureus | - |
- |
- |
2.3.2.18 | Staphylococcus aureus | - |
- |
- |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.2.16 | physiological function | surface protein is linked to tri- and monoglycyl cross-bridges of peptidoglycan isolated from femB and femA mutant staphylococci, respectively. No surface protein is found linked directly to the epsilon-amino group of lysyl within the cell wall of a femAX strain | Staphylococcus aureus |
2.3.2.17 | physiological function | surface protein is linked to tri- and monoglycyl cross-bridges of peptidoglycan isolated from femB and femA mutant staphylococci, respectively. No surface protein is found linked directly to the epsilon-amino group of lysyl within the cell wall of a femAX strain. Peptidoglycan analysis of a femAB mutant strain reveals the presence of pentaglycyl, tetraglycyl-monoseryl, and monoglycyl as well as small amounts of triglycyl cross-bridges. Analysis of anchor peptides shows that surface proteins are mostly linked to tetraglycylmonoseryl as well as pentaglycyl. The sortase activity of Staphylococcus aureus prefers cross-bridges containing five residues, but altered cell-wall cross-bridges can be linked to the COOH-terminal end of surface proteins | Staphylococcus aureus |
2.3.2.18 | physiological function | surface protein is linked to tri- and monoglycyl cross-bridges of peptidoglycan isolated from femB and femA mutant staphylococci, respectively. Peptidoglycan analysis of a femAB mutant strain reveals the presence of pentaglycyl, tetraglycyl-monoseryl, and monoglycyl as well as small amounts of triglycyl cross-bridges. Analysis of anchor peptides shows that surface proteins are mostly linked to tetraglycylmonoseryl as well as pentaglycyl. The sortase activity of Staphylococcus aureus prefers cross-bridges containing five residues, but altered cell-wall cross-bridges can be linked to the COOH-terminal end of surface proteins | Staphylococcus aureus |