ID   ENLYS_BPT1              Reviewed;         162 AA.
AC   Q6XQ98;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-SEP-2021, entry version 72.
DE   RecName: Full=SAR-endolysin {ECO:0000255|HAMAP-Rule:MF_04136};
DE            EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04136};
DE   AltName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04136};
DE   AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04136};
DE   AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04136};
DE   AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04136};
GN   ORFNames=12;
OS   Escherichia phage T1 (Bacteriophage T1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Drexlerviridae; Tunavirinae; Tunavirus.
OX   NCBI_TaxID=1921008;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14972552; DOI=10.1016/j.virol.2003.09.020;
RA   Roberts M.D., Martin N.L., Kropinski A.M.;
RT   "The genome and proteome of coliphage T1.";
RL   Virology 318:245-266(2004).
CC   -!- FUNCTION: Signal-arrest-release (SAR) endolysin with lysozyme activity
CC       that degrades host peptidoglycans and participates with the pinholin
CC       and spanin proteins in the sequential events which lead to programmed
CC       host cell lysis releasing the mature viral particles. Once the pinholin
CC       has permeabilized the host cell membrane, the SAR-endolysin is released
CC       into the periplasm where it breaks down the peptidoglycan layer.
CC       {ECO:0000255|HAMAP-Rule:MF_04136}.
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_04136};
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04136}; Single-pass type II membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04136}; Periplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_04136}. Note=Secreted as a signal-anchored, membrane-tethered,
CC       inactive endolysin which is subsequently refolded, activated and
CC       released by membrane depolarization driven by the pinholin.
CC       {ECO:0000255|HAMAP-Rule:MF_04136}.
CC   -!- DOMAIN: The signal-anchor, which may also be an uncleaved signal
CC       sequence tethers the SAR-endolysin to the membrane until the latter is
CC       depolarized by the holin, resulting in the escape of SAR-endolysin from
CC       the membrane. {ECO:0000255|HAMAP-Rule:MF_04136}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04136}.
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DR   EMBL; AY216660; AAP49987.1; -; Genomic_DNA.
DR   RefSeq; YP_003933.1; NC_005833.1.
DR   SMR; Q6XQ98; -.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   PRIDE; Q6XQ98; -.
DR   GeneID; 2772979; -.
DR   KEGG; vg:2772979; -.
DR   Proteomes; UP000001156; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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:InterPro.
DR   Gene3D; 1.10.530.40; -; 1.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   HAMAP; MF_04136; SAR_ENDOLYSIN; 1.
DR   InterPro; IPR034690; Endolysin_T4_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023347; Lysozyme_dom_sf.
DR   InterPro; IPR043688; SAR_endolysin-like.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW   Host cell inner membrane; Host cell lysis by virus; Host cell membrane;
KW   Host membrane; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Viral release from host cell.
FT   CHAIN           1..162
FT                   /note="SAR-endolysin"
FT                   /id="PRO_0000429257"
FT   TRANSMEM        7..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        27
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT   ACT_SITE        36
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
SQ   SEQUENCE   162 AA;  18331 MW;  438AC2665EAA67AD CRC64;
     MSLKNNVIGA SIGAALTLTP TLLERIEGIE YEVYYDIAGV PTVCSGITGP DVIPGKKYTK
     RECDALLIKH IGVAQRYVDK KVKVDIPVTM RASLYSFTFN VGTGAFGSST MLKLINQRKH
     KEACNQLWRW VYYYNPKTKK REVSRGIKNR RAEEYAYCVK EL