| IED ID | IndEnz0002005441 |
| Enzyme Type ID | protease005441 |
| Protein Name |
Morphogenesis protein 1 Gene product 13 gp13 Protein p13 Includes: Lysozyme-like glycosidase EC 3.2.1.- ; Probable metalloendopeptidase EC 3.4.-.- |
| Gene Name | 13 |
| Organism | Bacillus phage phi29 (Bacteriophage phi-29) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Salasmaviridae Picovirinae Salasvirus Bacillus phage phi29 (Bacteriophage phi-29) |
| Enzyme Sequence | MVYVSNKYLTMSEMKVNAQYILNYLSSNGWTKQAICGMLGNMQSESTINPGLWQNLDEGNTSLGFGLVQWTPASNYINWANSQGLPYKDMDSELKRIIWEVNNNAQWINLRDMTFKEYIKSTKTPRELAMIFLASYERPANPNQPERGDQAEYWYKNLSGGGGGGLQLAQFPMDIINISQGENGSFSHKGTLCIDFVGKTEKYPYYAPCDCTCVWRGDASAYLAWTSDKEVMCADGSVRYITWVNVHESPLPFDVGKKLKKGDLMGHTGIGGNVTGDHWHFNVIDGKEYQGWTKKPDSCLAGTELHIYDVFAVNNVEIINGNGYDWKTSDWQDGDGGDGDDDNDNNKTKDLITLLLSDALHGWKA |
| Enzyme Length | 365 |
| Uniprot Accession Number | P15132 |
| Absorption | |
| Active Site | ACT_SITE 45; /note=For lysozyme-like glycosidase activity; /evidence=ECO:0000305 |
| Activity Regulation | |
| Binding Site | BINDING 45; /note="Substrate"; /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0, ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5"; BINDING 71; /note="Substrate"; /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0, ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5"; BINDING 106; /note="Substrate"; /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0, ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.2.1.-; 3.4.-.- |
| Enzyme Function | FUNCTION: May serve as a plug to restrain the highly pressurized packaged genome and thus would be the first virion protein to contact the host cell wall, degrading the peptidoglycan layer and thereby facilitating viral genome entry into the host bacteria. Acts probably as a multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall. Essential for the tail assembly. {ECO:0000305|PubMed:18394643, ECO:0000305|PubMed:18606992}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (15); Binding site (3); Chain (1); Helix (9); Metal binding (3); Region (4); Sequence conflict (2); Turn (4) |
| Keywords | 3D-structure;Antimicrobial;Bacteriolytic enzyme;Cell wall biogenesis/degradation;Degradation of host cell envelope components during virus entry;Degradation of host peptidoglycans during virus entry;Glycosidase;Hydrolase;Late protein;Metal-binding;Metalloprotease;Multifunctional enzyme;Protease;Reference proteome;Viral genome ejection through host cell envelope;Viral penetration into host cytoplasm;Viral release from host cell;Viral short tail ejection system;Viral tail assembly;Virion;Virus entry into host cell;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:18394643, ECO:0000269|PubMed:18606992}. Note=Located at the distal tip of the tail knob. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 3CSQ; 3CSR; 3CSZ; 3CT0; 3CT1; 3CT5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,925 |
| Kinetics | |
| Metal Binding | METAL 188; /note=Zinc; /evidence=ECO:0007744|PDB:3CSQ; METAL 195; /note=Zinc; /evidence=ECO:0007744|PDB:3CSQ; METAL 280; /note=Zinc; /evidence=ECO:0007744|PDB:3CSQ |
| Rhea ID | |
| Cross Reference Brenda |