ID   ENLYS_BPVT2             Reviewed;         177 AA.
AC   P68921; Q9T0Q1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   02-SEP-2026, entry version 75.
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   Name=R;
OS   Enterobacteria phage VT2-Sa (Bacteriophage VT2-Sa).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudoviricetes incertae sedis; Sepvirinae; Traversvirus; Traversvirus II.
OX   NCBI_TaxID=97081;
OH   NCBI_TaxID=83334; Escherichia coli O157:H7.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10492170; DOI=10.1093/dnares/6.4.235;
RA   Miyamoto H., Nakai W., Yajima N., Fujibayashi A., Higuchi T., Sato K.,
RA   Matsushiro A.;
RT   "Sequence analysis of Stx2-converting phage VT2-Sa shows a great divergence
RT   in early regulation and replication regions.";
RL   DNA Res. 6:235-240(1999).
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; AP000363; BAA84328.1; -; Genomic_DNA.
DR   RefSeq; NP_050544.1; NC_000902.1.
DR   SMR; P68921; -.
DR   GeneID; 1262225; -.
DR   KEGG; vg:1262225; -.
DR   OrthoDB; 18172at10239; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd16900; endolysin_R21-like; 1.
DR   Gene3D; 1.10.530.40; -; 1.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   HAMAP; MF_04136; SAR_ENDOLYSIN; 1.
DR   InterPro; IPR051018; Bacteriophage_GH24.
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   PANTHER; PTHR38107; -; 1.
DR   PANTHER; PTHR38107:SF3; LYSOZYME RRRD-RELATED; 1.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral release from host cell.
FT   CHAIN           1..177
FT                   /note="SAR-endolysin"
FT                   /id="PRO_0000218090"
FT   TRANSMEM        1..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        35
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT   ACT_SITE        44
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
SQ   SEQUENCE   177 AA;  19607 MW;  E546FDCB1201F036 CRC64;
     MSRKLRYGLS AAVLALIAAG ASAPEILDQF LDEKEGNHTT AYRDGAGIWT ICRGATRVDG
     KPVIPGMKLS KEKCDRVNAI ERDKALAWVE KNIKVPLTEP QKAGIASFCP YNIGPGKCFP
     STFYRRINAG DRKGACEAIR WWIKDGGRDC RIRSNNCYGQ VSRRDQESAL ACWGIDR
//