|Family type peptidase||S74.001 - Escherichia coli phage K1F endosialidase CIMCD self-cleaving protein (Enterobacteria phage K1F), MEROPS Accession MER0151384 (peptidase unit: 911-1011)|
|Content of family||Family S74 contains serine endopeptidases|
Identifier created: MEROPS 9.5 (1 July 2011)|
During invasion of the host, a bacteriophage has to penetrate the cell wall and endosialidases are produced to hydrolyse the polysialic acid capsule. Endosialidase NF is synthesized as a precursor which a C-terminal propeptide which acts as a chaperone (Muhlenhoff et al., 2003). This propeptide is removed by a self-cleaving mechanism (Schulz et al., 2010).
|Active site residues||S911 K916 |
|Active site||A Ser, Lys catalytic dyad has been identified from the crystal structure (Schulz et al., 2010).|
|Molecular structure||The tertiary structure has been solved for the endo-N-acetylneuraminidase from enterobacteria phage K1F (Schultz et al., 2010). The fold is unlike that of any other peptidase, hence the fold of the C-terminal domain of endosialidase NF is the type structure for clan SO.|