ENLYS_BPHC1
ID ENLYS_BPHC1 Reviewed; 186 AA.
AC P51728;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 29-SEP-2021, entry version 94.
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=lys;
OS Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Peduovirinae; Hpunavirus.
OX NCBI_TaxID=1289570;
OH NCBI_TaxID=727; Haemophilus influenzae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6098523; DOI=10.1016/0378-1119(84)90208-7;
RA Benjamin R.C., Fitzmaurice W.P., Huang P.C., Scocca J.J.;
RT "Nucleotide sequence of cloned DNA segments of the Haemophilus influenzae
RT bacteriophage HP1c1.";
RL Gene 31:173-185(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8710508; DOI=10.1093/nar/24.12.2360;
RA Esposito D., Fitzmaurice W.P., Benjamin R.C., Goodman S.D., Waldman A.S.,
RA Scocca J.J.;
RT "The complete nucleotide sequence of bacteriophage HP1 DNA.";
RL Nucleic Acids Res. 24:2360-2368(1996).
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 -!- PTM: All the periplasmic cyteines of the inactive, membrane-associated
CC endolysin are involved in disulfide bond (By similarity). In the active
CC soluble form, disulfide bonds are isomerized and only the catalytic
CC cysteine remains free (By similarity). {ECO:0000250|UniProtKB:Q37875}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04136}.
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DR EMBL; U24159; AAB09211.1; -; Genomic_DNA.
DR PIR; S69532; S69532.
DR RefSeq; NP_043495.1; NC_001697.1.
DR SMR; P51728; -.
DR GeneID; 1261120; -.
DR KEGG; vg:1261120; -.
DR Proteomes; UP000001713; 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; Disulfide bond;
KW Glycosidase; Host cell inner membrane; Host cell lysis by virus;
KW Host cell membrane; Host membrane; Hydrolase; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix;
KW Viral release from host cell.
FT CHAIN 1..186
FT /note="SAR-endolysin"
FT /id="PRO_0000018519"
FT TRANSMEM 1..18
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT ACT_SITE 47
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT ACT_SITE 56
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT DISULFID 11..49
FT /note="In the active soluble endolysin"
FT /evidence="ECO:0000250|UniProtKB:Q37875"
FT DISULFID 49..56
FT /note="In the inactive membrane-associated endolysin"
FT /evidence="ECO:0000250|UniProtKB:Q37875"
SQ SEQUENCE 186 AA; 20553 MW; 0203E9A32EF45907 CRC64;
MSKKFGAMIL CSAAAVAAAF FAQQKGLPTQ QQNQVSPKAV SMIVNLEGCV RNPYKCPADV
WTNGVGNTHN VDKTKILTID EVATDLRRNI KEAENCINTY FNGEKMNQGQ YDAMVSLAFN
VGCGNIKTYY SKTQGKRVAT TIYRAAQAEN WILMCNRIED FNKSGGRVLK GLQNRRAKEK
ALCLGE
