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Protein

Lysozyme

Gene

17

Organism
Enterobacteria phage P1 (Bacteriophage P1)
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.By similarity

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 sitei42 – 421Proton donorBy 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
Protein gp17
Gene namesi
Name:17
Synonyms:lysa, lyz
OrganismiEnterobacteria phage P1 (Bacteriophage P1)
Taxonomic identifieri10678 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaePunalikevirus
Virus hostiEnterobacteriaceae [TaxID: 543]
ProteomesiUP000008091: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185LysozymePRO_0000218099Add
BLAST

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2511Combined sources
Helixi32 – 387Combined sources
Helixi41 – 466Combined sources
Helixi48 – 503Combined sources
Helixi53 – 553Combined sources
Beta strandi56 – 594Combined sources
Helixi74 – 9522Combined sources
Helixi98 – 1003Combined sources
Helixi103 – 11614Combined sources
Helixi118 – 1225Combined sources
Beta strandi123 – 1264Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1344Combined sources
Helixi136 – 1427Combined sources
Helixi146 – 1516Combined sources
Helixi152 – 1554Combined sources
Helixi165 – 17915Combined sources
Turni180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJTX-ray1.75A1-185[»]
1XJUX-ray1.07A/B29-185[»]
ProteinModelPortaliQ37875.
SMRiQ37875. Positions 9-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ37875.

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.

Q37875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGKTAAGGG AICAIAVMIT IVMGNGNVRT NQAGLELIGN AEGCRRDPYM
60 70 80 90 100
CPAGVWTDGI GNTHGVTPGV RKTDQQIAAD WEKNILIAER CINQHFRGKD
110 120 130 140 150
MPDNAFSAMT SAAFNMGCNS LRTYYSKARG MRVETSIHKW AQKGEWVNMC
160 170 180
NHLPDFVNSN GVPLRGLKIR REKERQLCLT GLVNE
Length:185
Mass (Da):20,256
Last modified:November 1, 1996 - v1
Checksum:i8F7CA469850049B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87673 Genomic DNA. Translation: CAA61013.1.
AF125376 Genomic DNA. Translation: AAD20630.1.
AF234172 Genomic DNA. Translation: AAQ13989.1.
RefSeqiYP_006484.1. NC_005856.1.

Genome annotation databases

GeneIDi2777454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87673 Genomic DNA. Translation: CAA61013.1.
AF125376 Genomic DNA. Translation: AAD20630.1.
AF234172 Genomic DNA. Translation: AAQ13989.1.
RefSeqiYP_006484.1. NC_005856.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XJTX-ray1.75A1-185[»]
1XJUX-ray1.07A/B29-185[»]
ProteinModelPortaliQ37875.
SMRiQ37875. Positions 9-185.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH24. Glycoside Hydrolase Family 24.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2777454.

Miscellaneous databases

EvolutionaryTraceiQ37875.

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

« Hide 'large scale' publications
  1. "Three functions of bacteriophage P1 involved in cell lysis."
    Schmidt C., Velleman M., Arber W.
    J. Bacteriol. 178:1099-1104(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Lehnherr H., Bendtsen J.D., Preuss F., Ilyina T.V.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiLYS_BPP1
AccessioniPrimary (citable) accession number: Q37875
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 75 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, Complete proteome, Reference proteome

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.