H
IPR036366

PGBD superfamily

InterPro entry
Short namePGBDSf
Overlapping entries
 

Description

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, 3, 2]
. 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]
.

References

1.Lysis genes of the Bacillus subtilis defective prophage PBSX. Krogh S, Jorgensen ST, Devine KM. J. Bacteriol. 180, 2110-7, (1998). View articlePMID: 9555893

2.Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. Foster SJ. J. Gen. Microbiol. 137, 1987-98, (1991). PMID: 1683402

3.Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution. Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM. Nature 299, 469-70, (1982). View articlePMID: 7121588

4.Active-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G. Charlier P, Dideberg O, Jamoulle JC, Frere JM, Ghuysen JM, Dive G, Lamotte-Brasseur J. Biochem. J. 219, 763-72, (1984). View articlePMID: 6743245

Cross References

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