Abstract
We identified a gene from Staphylococcus aureus, flp (fmtA-like protein), encoding a protein of 489 amino acid residues with a molecular mass of 56.4 kDa. The deduced amino acid sequence shows similarity to previously characterized penicillin binding proteins (PBPs) and FmtA of S. aureus (one of the factors which affect methicillin resistance). FLP protein has three motifs, which are conserved in PBPs and beta-lactamases, suggesting that it might be associated with cell wall synthesis. Recombinant FLP protein, however, lacks penicillin binding activity, and the inactivation of flp in two methicillin-resistant S. aureus strains did not cause a reduction in the methicillin resistance.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / genetics*
-
Bacterial Proteins / metabolism
-
Base Sequence
-
Carrier Proteins / genetics*
-
Carrier Proteins / metabolism
-
Cell Wall / metabolism
-
Hexosyltransferases*
-
Humans
-
Methicillin Resistance / genetics
-
Molecular Sequence Data
-
Molecular Weight
-
Muramoylpentapeptide Carboxypeptidase / genetics*
-
Muramoylpentapeptide Carboxypeptidase / metabolism
-
Mutation
-
Penicillin-Binding Proteins
-
Peptidyl Transferases*
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / genetics
-
Recombinant Proteins / metabolism
-
Sequence Alignment
-
Sequence Analysis, DNA
-
Staphylococcus aureus / drug effects
-
Staphylococcus aureus / genetics*
-
beta-Lactamases / genetics*
-
beta-Lactamases / metabolism
Substances
-
Bacterial Proteins
-
Carrier Proteins
-
Penicillin-Binding Proteins
-
Recombinant Proteins
-
Peptidyl Transferases
-
Hexosyltransferases
-
Muramoylpentapeptide Carboxypeptidase
-
beta-Lactamases