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InterPro: IPR008044 Bacteriophage peptidoglycan hydrolase

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UniProtKB
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85 proteins
AccessionHelp IPR008044 Phage_PGN_hydro
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AbstractHelp

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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PANDIT: PF05382
Pfam Clan: CL0125.11

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Example proteinsHelp
O03979 Lysin

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002479 Putative cell wall binding repeat
IPR018337 Cell wall/choline-binding repeat
IPR008044 Bacteriophage peptidoglycan hydrolase
SWISS-MODEL
ModBase

PublicationsHelp
1. 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
2. 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
3. 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