Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation.
The femAB operon codes for two nearly identical approximately 50-kDa proteins involved in the formation of the staphylococcal pentaglycine interpeptide bridge. Sequencing and analysis of the femA region of mutants isolated by chemical mutagenesis and selection for lysostaphin resistance revealed point mutations leading to the expression of truncated FemA proteins. These femA mutants, although still producing an intact FemB, exhibited a phenotype identical as that described for femAB double mutants. Thus, FemA seems to be essential for the addition of glycine residues 2 and 3 only, whereas FemB is involved in the attachment of exclusively glycine residues 4 and 5. Although FemB has 39% identity with FemA, it cannot substitute for FemA. The FemA and FemB proteins seem to be highly specific in regard to the position of the glycine residues that they attach.
Ehlert
K
K
PH-Research Antiinfectives I, Bayer AG, Wuppertal, Germany.
Schröder
W
W
Labischinski
H
H
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D005998:Glycine / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D010457:Peptidoglycan / Q000096:biosynthesis*; D017354:Point Mutation; D017384:Sequence Deletion; D013211:Staphylococcus aureus / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; C096686:FemA protein, Bacteria; C102928:FemB protein, Staphylococcus epidermidis; D009842:Oligopeptides; D010457:Peptidoglycan; D005998:Glycine