ENLYS_BPPZA
ID ENLYS_BPPZA Reviewed; 258 AA.
AC P07540;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
DE AltName: Full=Protein p15;
GN Name=15;
OS Bacillus phage PZA (Bacteriophage PZA).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus; Bacillus virus PZA.
OX NCBI_TaxID=10757;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3095188; DOI=10.1016/0378-1119(86)90048-x;
RA Paces V., Vlcek C., Urbanek P.;
RT "Nucleotide sequence of the late region of Bacillus subtilis phage PZA, a
RT close relative of phi 29.";
RL Gene 44:107-114(1986).
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 -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding. {ECO:0000250|UniProtKB:P11187}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04110}.
CC -!- CAUTION: Lacks the conserved Asp active site. {ECO:0000255|HAMAP-
CC Rule:MF_04110}.
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DR EMBL; M11813; AAA88492.1; -; Genomic_DNA.
DR PIR; A26215; WMBP15.
DR SMR; P07540; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR PRIDE; P07540; -.
DR Proteomes; UP000000855; 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; cd00118; LysM; 2.
DR CDD; cd00737; lyz_endolysin_autolysin; 1.
DR Gene3D; 1.10.530.40; -; 1.
DR Gene3D; 3.10.350.10; -; 2.
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; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF00959; Phage_lysozyme; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW Host cell lysis by virus; Host cytoplasm; Hydrolase;
KW Viral release from host cell.
FT CHAIN 1..258
FT /note="Endolysin"
FT /id="PRO_0000218106"
FT ACT_SITE 15
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
SQ SEQUENCE 258 AA; 28052 MW; 1A57FC5334637169 CRC64;
MQISQAGINL IKSFEGLQLK AYKAVPTEKH YTIGYGHYGS DVSPRQVITA KQAEDMLRDD
VQAFVDGVNK ALKVSVTQNQ FDALVSFAYN VGLGAFRSSS LLEYLNEGRT ALAAAEFPRW
NKSGGKVYQG LVNRRAQEQA LFNSGTPKNV SRGTSSSKVT PKYKVKSGDN LTKIAKKHNT
TVATLLKLNP SIKDPNMIRV GQTINVTGSG GKTHKVKSGD TLSKIAVDNK TTVSRLMSLN
PEITNPNHIK VGQTIRLS
