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Analysis of the Peptidoglycan Hydrolase Complement of Lactococcus lactis: Identification of a Third N-Acetylglucosaminidase, AcmC

Carine Huard,^1, Guy Miranda,¹ Yulia Redko,^1, Françoise Wessner,¹ Simon J. Foster,² and Marie-Pierre Chapot-Chartier^1*

Unité de Biochimie et Structure des Protéines, INRA, 78352 Jouy-en-Josas Cedex, France,¹ Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom²

Received 5 November 2003/ Accepted 5 March 2004

The peptidoglycan hydrolase (PGH) complement of Lactococcus lactis was identified by amino acid sequence similarity searching of the L. lactis IL-1403 complete genome sequence. Five PGHs that are not encoded by prophages were detected, including the previously characterized AcmA and AcmB proteins. Four of these PGHs, AcmA to AcmD, contain a catalytic domain homologous to that of enterococcal muramidase, but they have different domain structures. The fifth one (YjgB) has sequence similarity with the active-site domain of peptidoglycan-specific endopeptidases. The three new PGH-encoding genes identified in this study are all actively transcribed in L. lactis subsp. cremoris MG1363. The relative abundance of their transcripts varied during growth and was maximal during the early exponential growth phase. The three encoded proteins have peptidoglycan-hydrolyzing activities which are detected only at acidic pHs by zymography. Like AcmA and AcmB, AcmC has N-acetylglucosaminidase activity rather than the N-acetylmuramidase activity predicted by sequence similarity.

Present address: AFSSA, LERPRA, 06902 Sophia-Antipolis Cedex, France.

Present address: Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.

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