ENLYS_BPP1
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 03-AUG-2022, entry version 105.
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 Caudovirales; Myoviridae; Punavirus.
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 PRIDE; Q37875; -.
DR GeneID; 2777454; -.
DR KEGG; vg:2777454; -.
DR EvolutionaryTrace; Q37875; -.
DR Proteomes; UP000008091; 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 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
