ID   ENLYS_BPB03             Reviewed;         263 AA.
AC   Q37896;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 110.
DE   RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04110};
DE            EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04110};
DE   AltName: Full=Protein p15;
GN   Name=15;
OS   Bacillus phage B103 (Bacteriophage B103).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Beecentumtrevirus.
OX   NCBI_TaxID=10778;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9358052; DOI=10.1016/s0378-1119(97)00363-6;
RA   Pecenkova T., Benes V., Paces J., Vlcek C., Paces V.;
RT   "Bacteriophage B103: complete DNA sequence of its genome and relationship
RT   to other Bacillus phages.";
RL   Gene 199:157-163(1997).
CC   -!- FUNCTION: Endolysin with lysozyme activity that degrades host
CC       peptidoglycans and participates with the holin and spanin proteins in
CC       the sequential events which lead to the programmed host cell lysis
CC       releasing the mature viral particles. Once the holin has permeabilized
CC       the host cell membrane, the endolysin can reach the periplasm and break
CC       down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_04110};
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}.
CC       Note=The endolysin is cytoplasmic, but can reach the periplasmic space
CC       with the help of the holins which disrupt the host cell membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_04110}.
CC   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding. {ECO:0000250|UniProtKB:P11187}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04110}.
CC   -!- CAUTION: Lacks the conserved Asp active site. {ECO:0000255|HAMAP-
CC       Rule:MF_04110}.
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DR   EMBL; X99260; CAA67646.1; -; Genomic_DNA.
DR   RefSeq; NP_690649.1; NC_004165.1.
DR   SMR; Q37896; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   GeneID; 955364; -.
DR   KEGG; vg:955364; -.
DR   Proteomes; UP000000971; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd00118; LysM; 2.
DR   CDD; cd00737; lyz_endolysin_autolysin; 1.
DR   Gene3D; 1.10.530.40; -; 1.
DR   Gene3D; 3.10.350.10; -; 2.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   InterPro; IPR033907; Endolysin_autolysin.
DR   InterPro; IPR034690; Endolysin_T4_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023347; Lysozyme_dom_sf.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF54106; SSF54106; 2.
DR   PROSITE; PS51782; LYSM; 2.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW   Host cell lysis by virus; Host cytoplasm; Hydrolase;
KW   Viral release from host cell.
FT   CHAIN           1..263
FT                   /note="Endolysin"
FT                   /id="PRO_0000218092"
FT   ACT_SITE        15
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
SQ   SEQUENCE   263 AA;  29264 MW;  5C1A7C8282A1DBCE CRC64;
     MNISQAGINL IKSFEGLRTK AYKAVPTEKY YTIGYGHYGS DVHPCQVISE EKAEKLLRDD
     VQEFVDGVDK LLKVDVTQSQ FDALVSFAYN VGLGALKSST LLQYLNAGNF QKAANEFLKW
     NKSGGKVYNG LVKRREQERT LFLTGESKNV SRETSKPKTS KTNTHVVKKG DTLSEIAKKI
     KTSTKTLLEL NPTIKNPNKI YVGQRINVGG SPVKSTLKYK IKRGETLTGI AKKNKTTVSQ
     LMKLNPNIKN ANNIYAGQTI RLK