In this preliminary report we show that a 29 kDa surface protein of Listeria monocytogenes EGD removed from cells with 4 M LiCl has peptidoglycan (murein) hydrolyzing activity, as revealed by zymographic analysis using Bacillus subtilis murein and heat-killed Micrococcus luteus cells casted in the gel. Following two-dimensional electrophoresis, the protein was electroblotted to PVDF membrane and its identity (FlaA) was revealed by sequencing. Peptidoglycan hydrolysing activity of FlaA purified by FPLC on Mono-S Sepharose against labelled Escherichia coli murein was demonstrated.