ENLYS_BPP21
ID ENLYS_BPP21 Reviewed; 165 AA.
AC P27359;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 29-SEP-2021, entry version 86.
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 P21 (Bacteriophage 21) (Bacteriophage P21).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10711;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2019562; DOI=10.1128/jb.173.9.2897-2905.1991;
RA Bonovich M.T., Young R.;
RT "Dual start motif in two lambdoid S genes unrelated to lambda S.";
RL J. Bacteriol. 173:2897-2905(1991).
RN [2] {ECO:0007744|PDB:3HDE, ECO:0007744|PDB:3HDF}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 27-165, AND MUTAGENESIS OF
RP 14-GLY-GLY-15.
RX PubMed=19881499; DOI=10.1038/nsmb.1681;
RA Sun Q., Kuty G.F., Arockiasamy A., Xu M., Young R., Sacchettini J.C.;
RT "Regulation of a muralytic enzyme by dynamic membrane topology.";
RL Nat. Struct. Mol. Biol. 16:1192-1194(2009).
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; M65239; AAA32350.1; -; Genomic_DNA.
DR PDB; 3HDE; X-ray; 1.95 A; A/B/C/D=1-165.
DR PDB; 3HDF; X-ray; 1.70 A; A/B=27-165.
DR PDBsum; 3HDE; -.
DR PDBsum; 3HDF; -.
DR SMR; P27359; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR EvolutionaryTrace; P27359; -.
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; 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..165
FT /note="SAR-endolysin"
FT /id="PRO_0000218101"
FT TRANSMEM 8..28
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 ECO:0000305|PubMed:19881499"
FT ACT_SITE 44
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04136,
FT ECO:0000305|PubMed:19881499"
FT MUTAGEN 14..15
FT /note="GG->LL: The SAR-endolysin remains tethered in the
FT membrane and cannot be released; complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:19881499"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:3HDE"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3HDE"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3HDE"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3HDE"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3HDF"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3HDF"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:3HDF"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3HDF"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3HDF"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:3HDF"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3HDF"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3HDF"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3HDF"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3HDF"
SQ SEQUENCE 165 AA; 17996 MW; 14ECECD883232D3C CRC64;
MPPSLRKAVA AAIGGGAIAI ASVLITGPSG NDGLEGVSYI PYKDIVGVWT VCHGHTGKDI
MLGKTYTKAE CKALLNKDLA TVARQINPYI KVDIPETMRG ALYSLLYNVG AGNFRTSTLL
RKINQGDIKG ACDQLRRWTY AGGKQWKGLM TRREIEREIC LWGQQ
