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InterPro: IPR008044 Bacteriophage peptidoglycan hydrolase
Protein matches
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UniProtKB Matches: 85 proteins |
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Accession
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IPR008044 Phage_PGN_hydro |
Type
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Domain |
Signatures
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InterPro annotation
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Entry Details in BioMart
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Abstract
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At least one of the members of this domain, the Pal protein from the pneumococcal
bacteriophage Dp-1 O03979 has been shown to be an
N-acetylmuramoyl-L-alanine amidase [1]. According to the known modular
structure of this and other peptidoglycan hydrolases from the pneumococcal system, the active site
should reside in the N-terminal domain whereas the C-terminal domain binds to the choline residues
of the cell wall teichoic acids [2, 3].
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Database links
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Pfam Clan: CL0125.11
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Publications
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1.
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Garcia P, Mendez E, Garcia E, Ronda C, Lopez R.
Biochemical characterization of a murein hydrolase induced by bacteriophage Dp-1 in Streptococcus pneumoniae: comparative study between bacteriophage-associated lysin and the host amidase.
J. Bacteriol. 159 793-6 1984
[PubMed: 6146601]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=6146601
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2.
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Sheehan MM, Garcia JL, Lopez R, Garcia P.
The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin.
Mol. Microbiol. 25 717-25 1997
[PubMed: 9379901]
http://dx.doi.org/10.1046/j.1365-2958.1997.5101880.x
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3.
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Garcia E, Garcia JL, Garcia P, Arraras A, Sanchez-Puelles JM, Lopez R.
Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages.
Proc. Natl. Acad. Sci. U.S.A. 85 914-8 1988
[PubMed: 3422470]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=3422470
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InterPro 23.1
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