Protein Variants | Comment | Organism |
---|---|---|
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 |
Organism | UniProt | Comment | Textmining |
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Staphylococcus aureus | - |
- |
- |
General Information | Comment | Organism |
---|---|---|
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 |