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Protein

Lysozyme

Gene

R

Organism
Enterobacteria phage P21 (Bacteriophage 21) (Bacteriophage P21)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351Proton donorBy similarity
Active sitei44 – 441NucleophileBy similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH24. Glycoside Hydrolase Family 24.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
Endolysin
Lysis protein
Muramidase
Gene namesi
Name:R
OrganismiEnterobacteria phage P21 (Bacteriophage 21) (Bacteriophage P21)
Taxonomic identifieri10711 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiSalmonella [TaxID: 590]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165LysozymePRO_0000218101Add
BLAST

Expressioni

Keywords - Developmental stagei

Late protein

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi13 – 153Combined sources
Helixi16 – 2611Combined sources
Beta strandi30 – 356Combined sources
Beta strandi38 – 436Combined sources
Beta strandi49 – 524Combined sources
Helixi68 – 8619Combined sources
Helixi87 – 893Combined sources
Helixi96 – 10914Combined sources
Helixi114 – 12512Combined sources
Helixi128 – 1369Combined sources
Turni139 – 1413Combined sources
Beta strandi148 – 1503Combined sources
Helixi152 – 16312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HDEX-ray1.95A/B/C/D1-165[»]
3HDFX-ray1.70A/B27-165[»]
ProteinModelPortaliP27359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27359.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 24 family.Curated

Family and domain databases

Gene3Di1.10.530.40. 1 hit.
InterProiIPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
IPR023347. Lysozyme_dom.
[Graphical view]
PfamiPF00959. Phage_lysozyme. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

P27359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPSLRKAVA AAIGGGAIAI ASVLITGPSG NDGLEGVSYI PYKDIVGVWT
60 70 80 90 100
VCHGHTGKDI MLGKTYTKAE CKALLNKDLA TVARQINPYI KVDIPETMRG
110 120 130 140 150
ALYSLLYNVG AGNFRTSTLL RKINQGDIKG ACDQLRRWTY AGGKQWKGLM
160
TRREIEREIC LWGQQ
Length:165
Mass (Da):17,996
Last modified:August 1, 1992 - v1
Checksum:i14ECECD883232D3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65239 Genomic DNA. Translation: AAA32350.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65239 Genomic DNA. Translation: AAA32350.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HDEX-ray1.95A/B/C/D1-165[»]
3HDFX-ray1.70A/B27-165[»]
ProteinModelPortaliP27359.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH24. Glycoside Hydrolase Family 24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP27359.

Family and domain databases

Gene3Di1.10.530.40. 1 hit.
InterProiIPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
IPR023347. Lysozyme_dom.
[Graphical view]
PfamiPF00959. Phage_lysozyme. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Dual start motif in two lambdoid S genes unrelated to lambda S."
    Bonovich M.T., Young R.
    J. Bacteriol. 173:2897-2905(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiLYS_BPP21
AccessioniPrimary (citable) accession number: P27359
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.