Open AccessListeria monocytogenes EGD lacking penicillin‐binding protein 5 (PBP5) produces a thicker cell wall
Author(s) -
Korsak Dorota,
Vollmer Waldemar,
Markiewicz Zdzislaw
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2005.08.009
Subject(s) - listeria monocytogenes , penicillin binding proteins , penicillin , microbiology and biotechnology , cell wall , biology , bacteria , genetics , antibiotics
We report on the cloning of the structural gene for penicillin‐binding protein 5 (PBP5), lmo2754 . We also describe the enzymatic activity of PBP5 and characterize a mutant lacking this activity. Purified PBP5 has dd ‐carboxypeptidase activity, removing the terminal d ‐alanine residue from murein pentapeptide side chains. It shows higher activity against low molecular weight monomeric pentapeptide substrates compared to dimeric pentapeptide compound. Similarly, PBP5 preferentially cleaves monomeric pentapeptides present in high‐molecular weight murein sacculi. A Listeria monocytogenes mutant lacking functional PBP5 was constructed. Cells of the mutant are viable, showing that the protein is dispensable for growth, but grow slower and have thickened cell walls.