| IED ID | IndEnz0002011353 |
| Enzyme Type ID | protease011353 |
| Protein Name |
Morphogenesis protein 1 Late protein GP13 Includes: Lysozyme-like glycosidase EC 3.2.1.- ; Probable metalloendopeptidase EC 3.4.-.- |
| Gene Name | 13 |
| Organism | Bacillus phage B103 (Bacteriophage B103) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Salasmaviridae Picovirinae Beecentumtrevirus Bacillus phage B103 (Bacteriophage B103) |
| Enzyme Sequence | MFYSKNAYLSMKEMTVNAQYILNYLLPRGWTKNAICGMLGNMQTESTINPGIWQNLDEGNTSLGFGLVQWTPATKYLNWADRNGLKRDHMDSQLKRILWEVDNNEQWINLRNMTFKEFTKSTKSANELAMIFLASYERPANPNQPERGTQAEYWFKTLTGKGSTGIQLAQFPMDIINITQGENGSFSHKGTLCIDFVGKHEKYPYYAPCDCTCVWRGDESAYLAWTSDKEVMCADGTVRYITWVCVHDENLLYNVGKKLKKGELMGHSGKGGRATGDHLHLNVIEGNKYQGWVKKPDSALAGTELHIYDVFAVNGVEIVNGLGYDWKTSDWVDGSDENNGDDKDKDKDETKNIVNLLLCGALNGW |
| Enzyme Length | 365 |
| Uniprot Accession Number | Q37894 |
| Absorption | |
| Active Site | ACT_SITE 45; /note=For lysozyme-like glycosidase activity; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.2.1.-; 3.4.-.- |
| Enzyme Function | FUNCTION: Essential for tail assembly and the production of infectious particles (By similarity). Degrades the peptidoglycan layer of the host cell wall and thereby facilitates infection of host bacteria. Acts probably as multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Region (4) |
| Keywords | Antimicrobial;Bacteriolytic enzyme;Cell wall biogenesis/degradation;Glycosidase;Hydrolase;Late protein;Metal-binding;Metalloprotease;Multifunctional enzyme;Protease;Virion;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Located at the end of the tail structure. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,284 |
| Kinetics | |
| Metal Binding | METAL 188; /note=Zinc; /evidence=ECO:0000250; METAL 195; /note=Zinc; /evidence=ECO:0000250; METAL 280; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |