InterPro domain: IPR036366

This superfamily represents peptidoglycan binding domain (PGBD). PGBD may have a general peptidoglycan binding function. It has a core structure consisting of a closed, three-helical bundle with a left-handed twist. It is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation [ 1 , 2 , 3 ]. Examples are:

• Muramoyl-pentapeptide carboxypeptidase ( 3.4.17.8 )
• N-acetylmuramoyl-L-alanine amidase cwlA precursor (cell wall hydrolase, autolysin, 3.5.1.28 )
• Autolytic lysozyme (1,4-beta-N-acetylmuramidase, autolysin, 3.2.1.17 )
• Membrane-bound lytic murein transglycosylase B
• Zinc-containing D-alanyl-D-alanine-cleaving carboxypeptidase, VanX [ 4 ].

1. Lysis genes of the Bacillus subtilis defective prophage PBSX. J. Bacteriol. 180, 2110-7
2. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution. Nature 299, 469-70
3. Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. J. Gen. Microbiol. 137, 1987-98
4. Active-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G. Biochem. J. 219, 763-72