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Endolysin (EC 3.2.1.17) (Beta-1,4-N-acetylmuramidase) (Lysozyme) (Lytic enzyme) (Muramidase) (Protein P15)

 ENLYS_BPPRD             Reviewed;         149 AA.
P13559; Q3T4P3;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
25-OCT-2017, entry version 79.
RecName: Full=Endolysin;
EC=3.2.1.17 {ECO:0000269|PubMed:11741849, ECO:0000269|PubMed:7925454};
AltName: Full=Beta-1,4-N-acetylmuramidase;
AltName: Full=Lysozyme;
AltName: Full=Lytic enzyme;
AltName: Full=Muramidase;
AltName: Full=Protein P15;
Name=XV;
Enterobacteria phage PRD1 (Bacteriophage PRD1).
Viruses; dsDNA viruses, no RNA stage; Tectiviridae; Tectivirus.
NCBI_TaxID=10658;
NCBI_TaxID=471; Acinetobacter calcoaceticus.
NCBI_TaxID=562; Escherichia coli.
NCBI_TaxID=584; Proteus mirabilis.
NCBI_TaxID=287; Pseudomonas aeruginosa.
NCBI_TaxID=294; Pseudomonas fluorescens.
NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
NCBI_TaxID=90371; Salmonella typhimurium.
NCBI_TaxID=666; Vibrio cholerae.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2651121; DOI=10.1111/j.1432-1033.1989.tb14625.x;
Pakula T.M., Savilahti H., Bamford D.H.;
"Comparison of the amino acid sequence of the lytic enzyme from broad-
host-range bacteriophage PRD1 with sequences of other cell-wall-
peptidoglycan lytic enzymes.";
Eur. J. Biochem. 180:149-152(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
PubMed=3322943; DOI=10.1016/0378-1119(87)90183-1;
Savilahti H., Bamford D.H.;
"The complete nucleotide sequence of the left very early region of
Escherichia coli bacteriophage PRD1 coding for the terminal protein
and the DNA polymerase.";
Gene 57:121-130(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1853567; DOI=10.1016/0042-6822(91)90995-N;
Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M.,
Kalkkinen N., Frilander M., Bamford D.H.;
"Genome organization of membrane-containing bacteriophage PRD1.";
Virology 183:658-676(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
Bamford D.H., Bamford J.K.H.;
"A snapshot of viral evolution from genome analysis of the
tectiviridae family.";
J. Mol. Biol. 350:427-440(2005).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=7925454; DOI=10.1111/j.1432-1033.1994.00341.x;
Caldentey J., Hanninen A.L., Bamford D.H.;
"Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase
activity.";
Eur. J. Biochem. 225:341-346(1994).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=11741849; DOI=10.1128/JB.184.1.104-110.2002;
Rydman P.S., Bamford D.H.;
"The lytic enzyme of bacteriophage PRD1 is associated with the viral
membrane.";
J. Bacteriol. 184:104-110(2002).
-!- FUNCTION: Endolysin involved in host peptidoglycan digestion after
permeabilization of the cytoplasmic membrane by holin. Involved in
host cell lysis and liberation of progeny phages. Displays strong
lytic activity against chloroform-treated Gram-negative cells.
{ECO:0000269|PubMed:11741849, ECO:0000269|PubMed:7925454}.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins. {ECO:0000269|PubMed:11741849,
ECO:0000269|PubMed:7925454}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.0-8.0.;
Temperature dependence:
Inactivation temperature above 4 degrees Celsius.;
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000269|PubMed:11741849}; Peripheral membrane protein
{ECO:0000269|PubMed:11741849}. Note=May be associated with the
viral membrane via P20 and P22. {ECO:0000269|PubMed:11741849}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
{ECO:0000305}.
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EMBL; X14980; CAA33104.1; -; Genomic_DNA.
EMBL; M22161; AAA32451.1; -; Genomic_DNA.
EMBL; AY848689; AAX45908.1; -; Genomic_DNA.
PIR; S03568; LYBPD1.
RefSeq; NP_040683.1; NC_001421.2.
SMR; P13559; -.
GeneID; 1260935; -.
KEGG; vg:1260935; -.
Proteomes; UP000002143; Genome.
GO; GO:0055036; C:virion membrane; IDA:CACAO.
GO; GO:0003796; F:lysozyme activity; IDA:CACAO.
GO; GO:0051672; P:catabolism by organism of cell wall peptidoglycan in other organism; IDA:CACAO.
GO; GO:0044277; P:cell wall disassembly; IDA:CACAO.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0044659; P:cytolysis by virus of host cell; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
InterPro; IPR024408; Muramidase.
InterPro; IPR016284; Phage_PRD1_P15_lysozyme.
Pfam; PF11860; Muraidase; 1.
PIRSF; PIRSF001069; Lytic_enz_p15; 1.
1: Evidence at protein level;
Antimicrobial; Bacteriolytic enzyme; Complete proteome; Cytolysis;
Glycosidase; Host cell lysis by virus; Hydrolase; Membrane;
Reference proteome; Viral release from host cell; Virion.
CHAIN 1 149 Endolysin.
/FTId=PRO_0000165348.
SEQUENCE 149 AA; 17269 MW; 50ABB718032939B5 CRC64;
MQYTLWDIIS RVESNGNLKA LRFEPEYYQR RMERGDWDNS IIQNIRAANK CSLGTARMIY
CSSWGAVQIM GFNLYLNGAF NLSVAHFMEN EAYQVNEFRR FLLKNGLTEY TPERLASDKA
ARVKFAKVYN GAESYADLIL QACQFYGVK


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