Detail Information for IndEnz0010000548
IED ID IndEnz0010000548
Enzyme Type ID esterase000548
Protein Name Endolysin B
Gene 12 protein
Gp12
Mycolylarabinogalactan esterase
EC 3.1.-.-
Gene Name 12
Organism Mycobacterium phage D29 (Mycobacteriophage D29)
Taxonomic Lineage Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Siphoviridae (phages with long non-contractile tails) Fromanvirus Mycobacterium phage D29 (Mycobacteriophage D29)
Enzyme Sequence MSKPWLFTVHGTGQPDPLGPGLPADTARDVLDIYRWQPIGNYPAAAFPMWPSVEKGVAELILQIELKLDADPYADFAMAGYSQGAIVVGQVLKHHILPPTGRLHRFLHRLKKVIFWGNPMRQKGFAHSDEWIHPVAAPDTLGILEDRLENLEQYGFEVRDYAHDGDMYASIKEDDLHEYEVAIGRIVMKASGFIGGRDSVVAQLIELGQRPITEGIALAGAIIDALTFFARSRMGDKWPHLYNRYPAVEFLRQI
Enzyme Length 254
Uniprot Accession Number O64205
Absorption
Active Site ACT_SITE 82; /evidence="ECO:0000269|PubMed:19555454"; ACT_SITE 166; /evidence="ECO:0000305|PubMed:19555454"; ACT_SITE 240; /evidence="ECO:0000269|PubMed:19555454, ECO:0000305"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.-.-
Enzyme Function FUNCTION: Endolysin that degrades the junction between mycolic acid and peptidoglycans in the host cell wall and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the mycolic acid-rich outer membrane. Cleaves the ester linkage joining the mycolic acid-rich outer membrane to arabinogalactan, releasing free mycolic acids. {ECO:0000269|PubMed:19555454}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (10); Chain (1); Helix (11); Mutagenesis (1); Turn (1)
Keywords 3D-structure;Antimicrobial;Bacteriolytic enzyme;Cytolysis;Host cell lysis by virus;Hydrolase;Reference proteome;Viral release from host cell
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3HC7;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 28,512
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda