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Literature summary for 2.3.2.17 extracted from

  • Ehlert, K.; Schroder, W.; Labischinski, H.
    Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation (1997), J. Bacteriol., 179, 7573-7576.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
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General Information

General Information Comment Organism
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