ID   LYSB_BPML5              Reviewed;         254 AA.
AC   Q05328;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   07-OCT-2020, entry version 65.
DE   RecName: Full=Endolysin B {ECO:0000250|UniProtKB:O64205};
DE   AltName: Full=Gene 12 protein {ECO:0000305};
DE   AltName: Full=Gp12 {ECO:0000305};
DE   AltName: Full=Mycolylarabinogalactan esterase {ECO:0000250|UniProtKB:O64205};
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:O64205};
GN   Name=12;
OS   Mycobacterium phage L5 (Mycobacteriophage L5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Fromanvirus.
OX   NCBI_TaxID=31757;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8459766; DOI=10.1111/j.1365-2958.1993.tb01131.x;
RA   Hatfull G.F., Sarkis G.J.;
RT   "DNA sequence, structure and gene expression of mycobacteriophage L5: a
RT   phage system for mycobacterial genetics.";
RL   Mol. Microbiol. 7:395-405(1993).
CC   -!- FUNCTION: Endolysin that degrades the junction between mycolic acid and
CC       peptidoglycans in the host cell wall and participates with the holin
CC       protein in the sequential events which lead to the programmed host cell
CC       lysis releasing the mature viral particles. Once the holin has
CC       permeabilized the host cell membrane, the endolysin can reach the
CC       periplasm and break down the mycolic acid-rich outer membrane. Cleaves
CC       the ester linkage joining the mycolic acid-rich outer membrane to
CC       arabinogalactan, releasing free mycolic acids.
CC       {ECO:0000250|UniProtKB:O64205}.
CC   -!- SIMILARITY: Belongs to the L5likevirus endolysin B protein family.
CC       {ECO:0000305}.
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DR   EMBL; Z18946; CAA79388.1; -; Genomic_DNA.
DR   PIR; S30957; S30957.
DR   RefSeq; NP_039676.1; NC_001335.1.
DR   SMR; Q05328; -.
DR   ESTHER; bpml5-vg12; Lysin_B_C_ter.
DR   GeneID; 2942933; -.
DR   KEGG; vg:2942933; -.
DR   Proteomes; UP000002123; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1120; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR041855; Lysin_B_C_ter.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Host cell lysis by virus;
KW   Hydrolase; Reference proteome; Viral release from host cell.
FT   CHAIN           1..254
FT                   /note="Endolysin B"
FT                   /id="PRO_0000164713"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000250|UniProtKB:O64205"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250|UniProtKB:O64205"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000250|UniProtKB:O64205"
SQ   SEQUENCE   254 AA;  28847 MW;  8627B76D26E42360 CRC64;
     MSKPWLFTVH GTGQPDPLGP GLPADTARDV LDIYRWQPIG NYPAAAFPMW PSVEKGVAEL
     ILQIELKLDA DPYADFALAG YSQGAIVVGQ VLKHHIINPR GRLHRFLHRL RKVIFWGNPM
     RQKGFAHTDE WIHQVAASDT MGILEDRLEN LEQYGFEVRD YAHDGDMYAS IKEDDMHEYE
     VAIGRIVMSA RRFIGGKDSV IAQLIELGQR PIWEGIAMAR AIIDALTFFA KSTQGPSWPH
     LYNRFPAVEF LRRI