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LysM peptidoglycan-binding domain-containing protein
The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation [1]. This domain may have a general peptidoglycan binding function. The structure of this domain is known [2]. [1]. 1352512. Modular design of the Enterococcus hirae muramidase-2 and. Streptococcus faecalis autolysin.. Joris B, Englebert S, Chu CP, Kariyama R, Daneo-Moore L,. Shockman GD, Ghuysen JM;. FEMS Microbiol Lett 1992;70:257-264.. [2]. 10843862. The structure of a LysM domain from E. coli membrane-bound lytic. murein transglycosylase D (MltD).. Bateman A, Bycroft M;. J Mol Biol 2000;299:1113-1119. (from Pfam)
peptidoglycan DD-metalloendopeptidase family protein
Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown. (from Pfam)
M23 family metallopeptidase
M23 family metallopeptidase lyses bacterial cell wall peptidoglycans
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