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P13559 (VLYS_BPPRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme

EC=3.2.1.17
Alternative name(s):
Lytic enzyme
Muramidase
Protein P15
Gene names
Name:XV
OrganismEnterobacteria phage PRD1 (Bacteriophage PRD1) [Reference proteome]
Taxonomic identifier10658 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageTectiviridaeTectivirus
Virus hostAcinetobacter calcoaceticus [TaxID: 471]
Escherichia coli [TaxID: 562]
Proteus mirabilis [TaxID: 584]
Pseudomonas aeruginosa [TaxID: 287]
Pseudomonas fluorescens [TaxID: 294]
Pseudomonas putida (Arthrobacter siderocapsulatus) [TaxID: 303]
Salmonella typhimurium [TaxID: 90371]
Vibrio cholerae [TaxID: 666]

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.5 Ref.6

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.

Subcellular location

Virion membrane; Peripheral membrane protein. Note: May be associated with the viral membrane via P20 and P22. Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 24 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0-8.0.

Temperature dependence:

Inactivation temperature above 4 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Lysozyme
PRO_0000165348

Sequences

Sequence LengthMass (Da)Tools
P13559 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 50ABB718032939B5

FASTA14917,269
        10         20         30         40         50         60 
MQYTLWDIIS RVESNGNLKA LRFEPEYYQR RMERGDWDNS IIQNIRAANK CSLGTARMIY 

        70         80         90        100        110        120 
CSSWGAVQIM GFNLYLNGAF NLSVAHFMEN EAYQVNEFRR FLLKNGLTEY TPERLASDKA 

       130        140 
ARVKFAKVYN GAESYADLIL QACQFYGVK 

« Hide

References

[1]"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."
Pakula T.M., Savilahti H., Bamford D.H.
Eur. J. Biochem. 180:149-152(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete nucleotide sequence of the left very early region of Escherichia coli bacteriophage PRD1 coding for the terminal protein and the DNA polymerase."
Savilahti H., Bamford D.H.
Gene 57:121-130(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
[3]"Genome organization of membrane-containing bacteriophage PRD1."
Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M., Kalkkinen N., Frilander M., Bamford D.H.
Virology 183:658-676(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"A snapshot of viral evolution from genome analysis of the tectiviridae family."
Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L., Bamford D.H., Bamford J.K.H.
J. Mol. Biol. 350:427-440(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase activity."
Caldentey J., Hanninen A.L., Bamford D.H.
Eur. J. Biochem. 225:341-346(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane."
Rydman P.S., Bamford D.H.
J. Bacteriol. 184:104-110(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14980 Genomic DNA. Translation: CAA33104.1.
M22161 Genomic DNA. Translation: AAA32451.1.
AY848689 Genomic DNA. Translation: AAX45908.1.
PIRLYBPD1. S03568.
RefSeqNP_040683.1. NC_001421.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1260935.

Family and domain databases

InterProIPR024408. DUF3380.
IPR016284. Phage_PRD1_P15_lysozyme.
[Graphical view]
PfamPF11860. DUF3380. 1 hit.
[Graphical view]
PIRSFPIRSF001069. Lytic_enz_p15. 1 hit.
ProtoNetSearch...

Entry information

Entry nameVLYS_BPPRD
AccessionPrimary (citable) accession number: P13559
Secondary accession number(s): Q3T4P3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1991
Last modified: February 19, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries