ID   ENLYS_BPP1              Reviewed;         185 AA.
AC   Q37875;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 110.
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=Gene product 17;
DE            Short=gp17;
DE   AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04136};
DE   AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000303|PubMed:15637279};
DE   AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04136};
GN   Name=17; Synonyms=lysa, lyz;
OS   Escherichia phage P1 (Bacteriophage P1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Punavirus; Punavirus P1.
OX   NCBI_TaxID=2886926;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8576044; DOI=10.1128/jb.178.4.1099-1104.1996;
RA   Schmidt C., Velleman M., Arber W.;
RT   "Three functions of bacteriophage P1 involved in cell lysis.";
RL   J. Bacteriol. 178:1099-1104(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lehnherr H., Bendtsen J.D., Preuss F., Ilyina T.V.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA   Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA   Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT   "Genome of bacteriophage P1.";
RL   J. Bacteriol. 186:7032-7068(2004).
RN   [4]
RP   FUNCTION, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX   PubMed=15090650; DOI=10.1073/pnas.0400957101;
RA   Xu M., Struck D.K., Deaton J., Wang I.N., Young R.;
RT   "A signal-arrest-release sequence mediates export and control of the phage
RT   P1 endolysin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6415-6420(2004).
RN   [5] {ECO:0007744|PDB:1XJT, ECO:0007744|PDB:1XJU}
RP   X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) OF 29-185, DISULFIDE BOND,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-13; CYS-44 AND CYS-51.
RX   PubMed=15637279; DOI=10.1126/science.1105143;
RA   Xu M., Arulandu A., Struck D.K., Swanson S., Sacchettini J.C., Young R.;
RT   "Disulfide isomerization after membrane release of its SAR domain activates
RT   P1 lysozyme.";
RL   Science 307:113-117(2005).
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, ECO:0000269|PubMed:15090650}.
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, ECO:0000305|PubMed:15637279}; Single-pass type II
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_04136,
CC       ECO:0000305|PubMed:15637279}; Periplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_04136, ECO:0000269|PubMed:15090650,
CC       ECO:0000305|PubMed:15637279}. Note=Secreted as a signal-anchored,
CC       membrane-tethered, inactive endolysin which is subsequently refolded,
CC       activated and released by membrane depolarization driven by the
CC       pinholin. {ECO:0000255|HAMAP-Rule:MF_04136,
CC       ECO:0000305|PubMed:15637279}.
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   -!- PTM: All the periplasmic cyteines of the inactive, membrane-associated
CC       endolysin are involved in disulfide bond. In the active soluble form,
CC       disulfide bonds are isomerized and only the catalytic cysteine remains
CC       free. {ECO:0000255|HAMAP-Rule:MF_04136, ECO:0000269|PubMed:15637279}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04136}.
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DR   EMBL; X87673; CAA61013.1; -; Genomic_DNA.
DR   EMBL; AF125376; AAD20630.1; -; Genomic_DNA.
DR   EMBL; AF234172; AAQ13989.1; -; Genomic_DNA.
DR   RefSeq; YP_006484.1; NC_005856.1.
DR   PDB; 1XJT; X-ray; 1.75 A; A=1-185.
DR   PDB; 1XJU; X-ray; 1.07 A; A/B=29-185.
DR   PDBsum; 1XJT; -.
DR   PDBsum; 1XJU; -.
DR   BMRB; Q37875; -.
DR   SMR; Q37875; -.
DR   DrugBank; DB04272; Citric acid.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   GeneID; 2777454; -.
DR   KEGG; vg:2777454; -.
DR   OrthoDB; 18172at10239; -.
DR   EvolutionaryTrace; Q37875; -.
DR   Proteomes; UP000008091; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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: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; cd16901; lyz_P1; 1.
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   PANTHER; PTHR38107; -; 1.
DR   PANTHER; PTHR38107:SF4; LYSOZYME; 1.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme; Cytolysis;
KW   Disulfide bond; Glycosidase; Host cell inner membrane;
KW   Host cell lysis by virus; Host cell membrane; Host membrane; Hydrolase;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Viral release from host cell.
FT   CHAIN           1..185
FT                   /note="SAR-endolysin"
FT                   /id="PRO_0000218099"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        7..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..185
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:15090650"
FT   ACT_SITE        42
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136,
FT                   ECO:0000305|PubMed:15637279"
FT   ACT_SITE        51
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136,
FT                   ECO:0000269|PubMed:15637279"
FT   DISULFID        13..44
FT                   /note="In the active soluble endolysin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136,
FT                   ECO:0000269|PubMed:15637279"
FT   DISULFID        44..51
FT                   /note="In the inactive membrane-associated endolysin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04136,
FT                   ECO:0000269|PubMed:15637279"
FT   MUTAGEN         13
FT                   /note="C->A,S: Complete loss of enzymatic activity although
FT                   still releases from the host inner membrane."
FT                   /evidence="ECO:0000269|PubMed:15637279"
FT   MUTAGEN         44
FT                   /note="C->S: No effect on enzymatic activity; when
FT                   associated with A-13 or S-13."
FT                   /evidence="ECO:0000269|PubMed:15637279"
FT   MUTAGEN         51
FT                   /note="C->D: No effect on enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:15637279"
FT   HELIX           15..25
FT                   /evidence="ECO:0007829|PDB:1XJT"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:1XJT"
FT   HELIX           74..95
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           103..116
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           118..122
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   TURN            127..130
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           146..151
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           152..155
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   HELIX           165..179
FT                   /evidence="ECO:0007829|PDB:1XJU"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:1XJU"
SQ   SEQUENCE   185 AA;  20256 MW;  8F7CA469850049B2 CRC64;
     MKGKTAAGGG AICAIAVMIT IVMGNGNVRT NQAGLELIGN AEGCRRDPYM CPAGVWTDGI
     GNTHGVTPGV RKTDQQIAAD WEKNILIAER CINQHFRGKD MPDNAFSAMT SAAFNMGCNS
     LRTYYSKARG MRVETSIHKW AQKGEWVNMC NHLPDFVNSN GVPLRGLKIR REKERQLCLT
     GLVNE
//