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P09963 (ENLYS_BPP22) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Endolysin

EC=3.2.1.17
Alternative name(s):
Lysis protein
Lysozyme
Muramidase
Gene names
Name:19
OrganismEnterobacteria phage P22 (Bacteriophage P22) [Reference proteome]
Taxonomic identifier10754 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeP22likevirus
Virus hostSalmonella typhimurium [TaxID: 90371]

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer By similarity.

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

Host cytoplasm Potential. Note: The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Endolysin
PRO_0000218102

Regions

Compositional bias136 – 1416Poly-Arg

Sites

Active site161Proton donor By similarity
Active site251Nucleophile By similarity

Secondary structure

....................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09963 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 3A16675AB1A635EB

FASTA14616,139
        10         20         30         40         50         60 
MMQISSNGIT RLKREEGERL KAYSDSRGIP TIGVGHTGKV DGNSVASGMT ITAEKSSELL 

        70         80         90        100        110        120 
KEDLQWVEDA ISSLVRVPLN QNQYDALCSL IFNIGKSAFA GSTVLRQLNL KNYQAAADAF 

       130        140 
LLWKKAGKDP DILLPRRRRE RALFLS 

« Hide

References

« Hide 'large scale' references
[1]"Phage P22 lysis genes: nucleotide sequences and functional relationships with T4 and lambda genes."
Rennell D., Poteete A.R.
Virology 143:280-289(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Sequence of the genome of Salmonella bacteriophage P22."
Vander Byl C.S., Kropinski A.M.B.
J. Bacteriol. 182:6472-6481(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Corrected sequence of the bacteriophage P22 genome."
Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W., Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A., Casjens S.R.
J. Bacteriol. 185:1475-1477(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Nucleotide sequence of the bacteriophage P22 gene 19 to 3 region: identification of a new gene required for lysis."
Casjens S., Eppler K., Parr R., Poteete A.R.
Virology 171:588-598(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-146.
[5]"Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme."
Mooers B.H., Matthews B.W.
Acta Crystallogr. D 62:165-176(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10997 Genomic DNA. Translation: AAA32266.1.
AF217253 Genomic DNA. Translation: AAF75040.1.
BK000583 Genomic DNA. Translation: DAA01040.1.
J04356 Genomic DNA. Translation: AAA88340.1.
PIRLZBP22. S22904.
RefSeqNP_059622.1. NC_002371.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ANVX-ray1.04A/B1-146[»]
2ANXX-ray1.04A/B1-146[»]
ProteinModelPortalP09963.
SMRP09963. Positions 1-146.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH24. Glycoside Hydrolase Family 24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1262838.

Family and domain databases

Gene3D1.10.530.40. 1 hit.
InterProIPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
IPR023347. Lysozyme_dom.
[Graphical view]
PfamPF00959. Phage_lysozyme. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP09963.

Entry information

Entry nameENLYS_BPP22
AccessionPrimary (citable) accession number: P09963
Secondary accession number(s): Q7PCD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 85 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries