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P27359 (LYS_BPP21) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 63. 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:
Lysozyme

EC=3.2.1.17
Alternative name(s):
Endolysin
Lysis protein
Muramidase
Gene names
Name:R
OrganismEnterobacteria phage P21 (Bacteriophage 21) (Bacteriophage P21)
Taxonomic identifier10711 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostSalmonella [TaxID: 590]

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Acts as a transglycosylase.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165Lysozyme
PRO_0000218101

Sites

Active site351Proton donor By similarity
Active site441Nucleophile By similarity

Secondary structure

.......................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27359 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 14ECECD883232D3C

FASTA16517,996
        10         20         30         40         50         60 
MPPSLRKAVA AAIGGGAIAI ASVLITGPSG NDGLEGVSYI PYKDIVGVWT VCHGHTGKDI 

        70         80         90        100        110        120 
MLGKTYTKAE CKALLNKDLA TVARQINPYI KVDIPETMRG ALYSLLYNVG AGNFRTSTLL 

       130        140        150        160 
RKINQGDIKG ACDQLRRWTY AGGKQWKGLM TRREIEREIC LWGQQ 

« Hide

References

[1]"Dual start motif in two lambdoid S genes unrelated to lambda S."
Bonovich M.T., Young R.
J. Bacteriol. 173:2897-2905(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65239 Genomic DNA. Translation: AAA32350.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HDEX-ray1.95A/B/C/D1-165[»]
3HDFX-ray1.70A/B27-165[»]
ProteinModelPortalP27359.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH24. Glycoside Hydrolase Family 24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceP27359.

Entry information

Entry nameLYS_BPP21
AccessionPrimary (citable) accession number: P27359
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 16, 2013
This is version 63 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