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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)
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