ENLYS_BPPH2
ID ENLYS_BPPH2 Reviewed; 258 AA.
AC P11187; B3VMQ1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 29-SEP-2021, entry version 117.
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 phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027653; DOI=10.1093/nar/14.24.10001;
RA Garvey K.J., Saedi M.S., Ito J.;
RT "Nucleotide sequence of Bacillus phage phi 29 genes 14 and 15: homology of
RT gene 15 with other phage lysozymes.";
RL Nucleic Acids Res. 14:10001-10008(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-258.
RX PubMed=3879485; DOI=10.1016/0378-1119(85)90054-x;
RA Garvey K.J., Saedi M.S., Ito J.;
RT "The complete sequence of Bacillus phage phi 29 gene 16: a protein required
RT for the genome encapsidation reaction.";
RL Gene 40:311-316(1985).
RN [5]
RP PROTEIN SEQUENCE OF 1-15, CHARACTERIZATION, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=3469652; DOI=10.1073/pnas.84.4.955;
RA Saedi M.S., Garvey K.J., Ito J.;
RT "Cloning and purification of a unique lysozyme produced by Bacillus phage
RT phi 29.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:955-958(1987).
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 ECO:0000269|PubMed:3469652}.
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 ECO:0000269|PubMed:3469652};
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.
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; X04962; CAA28632.1; -; Genomic_DNA.
DR EMBL; M14782; AAA32288.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96038.1; -; Genomic_DNA.
DR EMBL; M14431; AAA88347.1; -; Genomic_DNA.
DR PIR; B24721; WMBPP9.
DR RefSeq; YP_002004544.1; NC_011048.1.
DR SMR; P11187; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 6446520; -.
DR KEGG; vg:6446520; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IMP:CACAO.
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 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Direct protein sequencing;
KW Glycosidase; Host cell lysis by virus; Host cytoplasm; Hydrolase;
KW Reference proteome; Viral release from host cell.
FT CHAIN 1..258
FT /note="Endolysin"
FT /id="PRO_0000218103"
FT ACT_SITE 15
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04110"
SQ SEQUENCE 258 AA; 28054 MW; 26AE0C1D927B42D8 CRC64;
MQISQAGINL IKSFEGLQLK AYKAVPTEKH YTIGYGHYGS DVSPRQVITA KQAEDMLRDD
VQAFVDGVNK ALKVSVTQNQ FDALVSFAYN VGLGAFRSSS LLEYLNEGRT ALAAAEFPKW
NKSGGKVYQG LINRRAQEQA LFNSGTPKNV SRGTSSTKTT PKYKVKSGDN LTKIAKKHNT
TVATLLKLNP SIKDPNMIRV GQTINVTGSG GKTHKVKSGD TLSKIAVDNK TTVSRLMSLN
PEITNPNHIK VGQTIRLS
