ID   ENLYS_BPMD2             Reviewed;         493 AA.
AC   O64203;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-FEB-2022, entry version 62.
DE   RecName: Full=Endolysin A {ECO:0000303|PubMed:24627486};
DE            EC=3.-.-.- {ECO:0000269|PubMed:24627486};
DE   AltName: Full=Gene 10 protein {ECO:0000305};
DE   AltName: Full=Gp10 {ECO:0000305};
DE   AltName: Full=Lysis protein {ECO:0000305};
DE   AltName: Full=Lysozyme {ECO:0000305};
GN   Name=10;
OS   Mycobacterium phage D29 (Mycobacteriophage D29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Fromanvirus.
OX   NCBI_TaxID=28369;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA   Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT   "Genome structure of mycobacteriophage D29: implications for phage
RT   evolution.";
RL   J. Mol. Biol. 279:143-164(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=24627486; DOI=10.1074/jbc.m113.529594;
RA   Pohane A.A., Joshi H., Jain V.;
RT   "Molecular dissection of phage endolysin: an interdomain interaction
RT   confers host specificity in Lysin A of Mycobacterium phage D29.";
RL   J. Biol. Chem. 289:12085-12095(2014).
CC   -!- FUNCTION: Endolysin that degrades host peptidoglycans and participates
CC       with the holin protein in the sequential events which lead to the
CC       programmed host cell lysis releasing the mature viral particles. Once
CC       the holin has permeabilized the host cell membrane, the endolysin can
CC       reach the periplasm and break down the peptidoglycan layer.
CC       {ECO:0000269|PubMed:24627486, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the L5likevirus endolysin A protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF022214; AAC18450.1; -; Genomic_DNA.
DR   PIR; G72800; G72800.
DR   RefSeq; NP_046825.1; NC_001900.1.
DR   SMR; O64203; -.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   GeneID; 1261629; -.
DR   KEGG; vg:1261629; -.
DR   Proteomes; UP000002131; 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   GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:UniProtKB.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Host cell lysis by virus;
KW   Hydrolase; Reference proteome; Viral release from host cell.
FT   CHAIN           1..493
FT                   /note="Endolysin A"
FT                   /id="PRO_0000164708"
SQ   SEQUENCE   493 AA;  54822 MW;  6292E851C4AD7AE1 CRC64;
     MTLIVTRDHA QWVHDMCRAR AGNRYGYGGA FTLNPRDTTD CSGLVLQTAA WYGGRKDWIG
     NRYGSTESFR LDHKIVYDLG FRRLPPGGVA ALGFTPVMLV GLQHGGGGRY SHTACTLMTM
     DIPGGPVKVS QRGVDWESRG EVNGVGVFLY DGARAWNDPL FHDFWYLDAK LEDGPTQSVD
     AAEILARATG LAYNRAVALL PAVRDGLIQA DCTNPNRIAM WLAQIGHESD DFKATAEYAS
     GDAYDTRTDL GNTPEVDGDG RLYKGRSWIM ITGKDNYRDF SRWAHGRGLV PTPDYFVVHP
     LELSELRWAG IGAAWYWTVE RPDINALSDR RDLETVTRRI NGGLTNLDDR RRRYNLALAV
     GDQLLTLIGD DDELADPTIQ RFIREIHGAL FNTVVTQSPY GDPQNPDGSE PRSNLWQLHE
     LIKNGDGMGH ARYVEESARA GDLRELERVV RAAKGLGRDR SPEFIARARN VLAQIEAANP
     EYLQAYIARN GAL