ENLYS_BPPRD
ID ENLYS_BPPRD Reviewed; 149 AA.
AC P13559; Q3T4P3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 23-FEB-2022, entry version 91.
DE RecName: Full=Endolysin;
DE EC=3.2.1.17 {ECO:0000269|PubMed:11741849, ECO:0000269|PubMed:7925454};
DE AltName: Full=Beta-1,4-N-acetylmuramidase;
DE AltName: Full=Lysozyme;
DE AltName: Full=Lytic enzyme;
DE AltName: Full=Muramidase;
DE AltName: Full=Protein P15;
GN Name=XV;
OS Enterobacteria phage PRD1 (Bacteriophage PRD1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Kalamavirales; Tectiviridae; Alphatectivirus.
OX NCBI_TaxID=10658;
OH NCBI_TaxID=471; Acinetobacter calcoaceticus.
OH NCBI_TaxID=562; Escherichia coli.
OH NCBI_TaxID=584; Proteus mirabilis.
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
OH NCBI_TaxID=294; Pseudomonas fluorescens.
OH NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
OH NCBI_TaxID=90371; Salmonella typhimurium.
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2651121; DOI=10.1111/j.1432-1033.1989.tb14625.x;
RA Pakula T.M., Savilahti H., Bamford D.H.;
RT "Comparison of the amino acid sequence of the lytic enzyme from broad-host-
RT range bacteriophage PRD1 with sequences of other cell-wall-peptidoglycan
RT lytic enzymes.";
RL Eur. J. Biochem. 180:149-152(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RX PubMed=3322943; DOI=10.1016/0378-1119(87)90183-1;
RA Savilahti H., Bamford D.H.;
RT "The complete nucleotide sequence of the left very early region of
RT Escherichia coli bacteriophage PRD1 coding for the terminal protein and the
RT DNA polymerase.";
RL Gene 57:121-130(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1853567; DOI=10.1016/0042-6822(91)90995-n;
RA Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M., Kalkkinen N.,
RA Frilander M., Bamford D.H.;
RT "Genome organization of membrane-containing bacteriophage PRD1.";
RL Virology 183:658-676(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
RA Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
RA Bamford D.H., Bamford J.K.H.;
RT "A snapshot of viral evolution from genome analysis of the tectiviridae
RT family.";
RL J. Mol. Biol. 350:427-440(2005).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7925454; DOI=10.1111/j.1432-1033.1994.00341.x;
RA Caldentey J., Hanninen A.L., Bamford D.H.;
RT "Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase
RT activity.";
RL Eur. J. Biochem. 225:341-346(1994).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=11741849; DOI=10.1128/jb.184.1.104-110.2002;
RA Rydman P.S., Bamford D.H.;
RT "The lytic enzyme of bacteriophage PRD1 is associated with the viral
RT membrane.";
RL J. Bacteriol. 184:104-110(2002).
CC -!- FUNCTION: Endolysin involved in host peptidoglycan digestion after
CC permeabilization of the cytoplasmic membrane by holin. Involved in host
CC cell lysis and liberation of progeny phages. Displays strong lytic
CC activity against chloroform-treated Gram-negative cells.
CC {ECO:0000269|PubMed:11741849, ECO:0000269|PubMed:7925454}.
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:0000269|PubMed:11741849,
CC ECO:0000269|PubMed:7925454};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0.;
CC Temperature dependence:
CC Inactivation temperature above 4 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:11741849};
CC Peripheral membrane protein {ECO:0000269|PubMed:11741849}. Note=May be
CC associated with the viral membrane via P20 and P22.
CC {ECO:0000269|PubMed:11741849}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family. {ECO:0000305}.
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DR EMBL; X14980; CAA33104.1; -; Genomic_DNA.
DR EMBL; M22161; AAA32451.1; -; Genomic_DNA.
DR EMBL; AY848689; AAX45908.1; -; Genomic_DNA.
DR PIR; S03568; LYBPD1.
DR RefSeq; NP_040683.1; NC_001421.2.
DR SMR; P13559; -.
DR Proteomes; UP000002143; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IDA:CACAO.
DR GO; GO:0003796; F:lysozyme activity; IDA:CACAO.
DR GO; GO:0033922; F:peptidoglycan beta-N-acetylmuramidase activity; IDA:CACAO.
DR GO; GO:0044277; P:cell wall disassembly; IDA:CACAO.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:CACAO.
DR InterPro; IPR024408; Muramidase.
DR InterPro; IPR016284; Phage_PRD1_P15_lysozyme.
DR Pfam; PF11860; Muramidase; 1.
DR PIRSF; PIRSF001069; Lytic_enz_p15; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Glycosidase;
KW Host cell lysis by virus; Hydrolase; Membrane; Reference proteome;
KW Viral release from host cell; Virion.
FT CHAIN 1..149
FT /note="Endolysin"
FT /id="PRO_0000165348"
SQ SEQUENCE 149 AA; 17269 MW; 50ABB718032939B5 CRC64;
MQYTLWDIIS RVESNGNLKA LRFEPEYYQR RMERGDWDNS IIQNIRAANK CSLGTARMIY
CSSWGAVQIM GFNLYLNGAF NLSVAHFMEN EAYQVNEFRR FLLKNGLTEY TPERLASDKA
ARVKFAKVYN GAESYADLIL QACQFYGVK
