ENLYS_BPPS3
ID ENLYS_BPPS3 Reviewed; 167 AA.
AC O80288;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 29-SEP-2021, entry version 68.
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 19;
DE Short=gp19;
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=19;
OS Bacteriophage PS34.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae.
OX NCBI_TaxID=83127;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zimmer A., Schmieger H.;
RT "Lysis gene modules in the phage P22 gene pool.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AJ011580; CAA09706.1; -; Genomic_DNA.
DR SMR; O80288; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
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; Signal-anchor; Transmembrane;
KW Transmembrane helix; Viral release from host cell.
FT CHAIN 1..167
FT /note="SAR-endolysin"
FT /id="PRO_0000218104"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT ACT_SITE 37
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
FT ACT_SITE 46
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136"
SQ SEQUENCE 167 AA; 18187 MW; B9DC214DA0382343 CRC64;
MAMSPAVRNS VIAAISGGAI AIASVLITGP GGNDGLEGVR YKPYKDVVGV LTVCYGHTGK
DIMPGKTYTE AECKALLNKD LATVARQINP YIKVDIPETT RGGIYSFVYN VGAGNFETST
LLRKINQVDI KGACDQLRRW TYAGGKQWKG LMTRREIERE VCLWGQQ
