RT Journal Article SR Electronic(1) A1 Huard, Carine A1 Miranda, Guy A1 Wessner, Françoise A1 Bolotin, Alexander A1 Hansen, Jonathan A1 Foster, Simon J. A1 Chapot-Chartier, Marie-PierreYR 2003 T1 Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis JF Microbiology, VO 149 IS 3 SP 695 OP 705 DO https://doi.org/10.1099/mic.0.25875-0 PB Microbiology Society, SN 1465-2080, AB A gene encoding a putative peptidoglycan hydrolase, named acmB, which is a paralogue of the major autolysin acmA gene, was identified in the Lactococcus lactis genome sequence. The acmB gene is transcribed in L. lactis MG1363 and its expression is modulated during cellular growth. The encoded AcmB protein has a modular structure with three domains: an N-terminal domain, especially rich in Ser, Thr, Pro and Asn residues, resembling a cell-wall-associated domain; a central domain homologous to the Enterococcus hirae muramidase catalytic domain; and a C-terminal domain of unknown function. A recombinant AcmB derivative, devoid of its N-terminal domain, was expressed in Escherichia coli. It exhibited hydrolysing activity on the peptidoglycan of several Gram-positive bacteria, including L. lactis. Though showing sequence similarity with enterococcal muramidase, AcmB has N-acetylglucosaminidase specificity. The acmB gene was inactivated in order to evaluate the role of the enzyme. AcmB does not appear to be involved in cell separation but contributes to cellular autolysis., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.25875-0