ENLYS_BPP22
ID ENLYS_BPP22 Reviewed; 146 AA.
AC P09963; Q7PCD5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 29-SEP-2021, entry version 115.
DE RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04110};
DE EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04110};
DE AltName: Full=Muramidase {ECO:0000255|HAMAP-Rule:MF_04110};
GN Name=19;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2998005; DOI=10.1016/0042-6822(85)90115-1;
RA Rennell D., Poteete A.R.;
RT "Phage P22 lysis genes: nucleotide sequences and functional relationships
RT with T4 and lambda genes.";
RL Virology 143:280-289(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-146.
RX PubMed=2763468; DOI=10.1016/0042-6822(89)90628-4;
RA Casjens S., Eppler K., Parr R., Poteete A.R.;
RT "Nucleotide sequence of the bacteriophage P22 gene 19 to 3 region:
RT identification of a new gene required for lysis.";
RL Virology 171:588-598(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS).
RX PubMed=16421448; DOI=10.1107/s0907444905037212;
RA Mooers B.H., Matthews B.W.;
RT "Extension to 2268 atoms of direct methods in the ab initio determination
RT of the unknown structure of bacteriophage P22 lysozyme.";
RL Acta Crystallogr. D 62:165-176(2006).
CC -!- FUNCTION: Endolysin with lysozyme activity that degrades host
CC peptidoglycans and participates with the holin and spanin proteins in
CC the sequential events which lead to the programmed host cell lysis
CC releasing the mature viral particles. Once the holin has permeabilized
CC the host cell membrane, the endolysin can reach the periplasm and break
CC down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04110}.
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_04110};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}.
CC Note=The endolysin is cytoplasmic, but can reach the periplasmic space
CC with the help of the holins which disrupt the host cell membrane.
CC {ECO:0000255|HAMAP-Rule:MF_04110}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04110}.
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DR EMBL; M10997; AAA32266.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75040.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA01040.1; -; Genomic_DNA.
DR EMBL; J04356; AAA88340.1; -; Genomic_DNA.
DR PIR; S22904; LZBP22.
DR RefSeq; NP_059622.1; NC_002371.2.
DR PDB; 2ANV; X-ray; 1.04 A; A/B=1-146.
DR PDB; 2ANX; X-ray; 1.04 A; A/B=1-146.
DR PDBsum; 2ANV; -.
DR PDBsum; 2ANX; -.
DR SMR; P09963; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 1262838; -.
DR KEGG; vg:1262838; -.
DR EvolutionaryTrace; P09963; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00737; lyz_endolysin_autolysin; 1.
DR Gene3D; 1.10.530.40; -; 1.
DR HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR InterPro; IPR033907; Endolysin_autolysin.
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 Pfam; PF00959; Phage_lysozyme; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; Cytolysis;
KW Direct protein sequencing; Glycosidase; Host cell lysis by virus;
KW Host cytoplasm; Hydrolase; Reference proteome;
KW Viral release from host cell.
FT CHAIN 1..146
FT /note="Endolysin"
FT /id="PRO_0000218102"
FT ACT_SITE 16
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
FT ACT_SITE 25
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2ANV"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:2ANV"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2ANV"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:2ANV"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:2ANV"
SQ SEQUENCE 146 AA; 16139 MW; 3A16675AB1A635EB CRC64;
MMQISSNGIT RLKREEGERL KAYSDSRGIP TIGVGHTGKV DGNSVASGMT ITAEKSSELL
KEDLQWVEDA ISSLVRVPLN QNQYDALCSL IFNIGKSAFA GSTVLRQLNL KNYQAAADAF
LLWKKAGKDP DILLPRRRRE RALFLS
