Protein Family Models

Described members of this protein family occur at the tip of tails of phi-29-like phage. The location suggests both lysozyme activity, as supported by the lysozyme-like fold, and a page morphogenetic function, consistent with experimental observations, as location at the tail tip could be important for plugging the tail tube and ensuring proper phage assembly.

Date:

2024-10-16

At least one of the members of this family, the Pal protein from the pneumococcal bacteriophage Dp-1 Swiss:O03979 has been shown to be a 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 at the N-terminal domain whereas the C-terminal domain binds to the choline residues of the cell wall teichoic acids [2,3]. This family appears to be related to Pfam:PF00877. [1]. 6146601. Biochemical characterization of a murein hydrolase induced by bacteriophage Dp-1 in Streptococcus pneumoniae: comparative study between bacteriophage-associated lysin and the host amidase. Garcia P, Mendez E, Garcia E, Ronda C, Lopez R;. J Bacteriol 1984;159:793-796. [2]. 9379901. The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin. Sheehan MM, Garcia JL, Lopez R, Garcia P;. Mol Microbiol 1997;25:717-725. [3]. 3422470. Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Garcia E, Garcia JL, Garcia P, Arraras A, Sanchez-Puelles JM, Lopez R;. Proc Natl Acad Sci U S A 1988;85:914-918. (from Pfam)

Date:

2024-10-16