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Protein

Endolysin

Gene

R

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

Functioni

Endolysin with transglycosylase 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.

Catalytic activityi

Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei19 – 1911 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Lyase

Keywords - Biological processi

Cytolysis, Host cell lysis by virus, Virus exit from host cell

Protein family/group databases

CAZyiGH104. Glycoside Hydrolase Family 104.

Names & Taxonomyi

Protein namesi
Recommended name:
Endolysin (EC:4.2.2.n2)
Alternative name(s):
Lysis protein
Lysozyme
Muramidase
Transglycosylase
Gene namesi
Name:R
OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
Taxonomic identifieri10710 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000001711 Componenti: Genome

Subcellular locationi

  • Host cytoplasm Curated

  • Note: The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311H → D: No effect on lytic activity. 1 Publication
Mutagenesisi31 – 311H → N: No effect on lytic activity; when associated with N-137. 1 Publication
Mutagenesisi48 – 481H → N: 97% loss of lytic activity. 1 Publication
Mutagenesisi137 – 1371H → N: No effect on lytic activity; when associated with N-31. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158EndolysinPRO_0000218108Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP03706. 1 interaction.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Beta strandi21 – 266Combined sources
Turni31 – 344Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 613Combined sources
Turni65 – 684Combined sources
Helixi71 – 8111Combined sources
Helixi88 – 10114Combined sources
Helixi105 – 1106Combined sources
Helixi113 – 1208Combined sources
Turni121 – 1233Combined sources
Beta strandi132 – 1343Combined sources
Helixi135 – 14814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AM7X-ray2.30A/B/C1-158[»]
1D9UX-ray2.60A/B1-154[»]
3D3DX-ray2.60A/B1-154[»]
ProteinModelPortaliP03706.
SMRiP03706. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03706.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 24 family.Curated

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P03706-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEINNQRKA FLDMLAWSEG TDNGRQKTRN HGYDVIVGGE LFTDYSDHPR
60 70 80 90 100
KLVTLNPKLK STGAGRYQLL SRWWDAYRKQ LGLKDFSPKS QDAVALQQIK
110 120 130 140 150
ERGALPMIDR GDIRQAIDRC SNIWASLPGA GYGQFEHKAD SLIAKFKEAG

GTVREIDV
Length:158
Mass (Da):17,825
Last modified:July 21, 1986 - v1
Checksum:i94F8E9A512EAA03E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741Missing AA sequence (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96598.1.
PIRiB04333. EYBPL.
RefSeqiNP_040645.1. NC_001416.1.

Genome annotation databases

GeneIDi2703480.
KEGGivg:2703480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02459 Genomic DNA. Translation: AAA96598.1.
PIRiB04333. EYBPL.
RefSeqiNP_040645.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AM7X-ray2.30A/B/C1-158[»]
1D9UX-ray2.60A/B1-154[»]
3D3DX-ray2.60A/B1-154[»]
ProteinModelPortaliP03706.
SMRiP03706. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03706. 1 interaction.

Protein family/group databases

CAZyiGH104. Glycoside Hydrolase Family 104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703480.
KEGGivg:2703480.

Miscellaneous databases

EvolutionaryTraceiP03706.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Amino-acid sequence of lambda phage endolysin."
    Imada M., Tsugita A.
    Nature New Biol. 233:230-231(1971)
    Cited for: PROTEIN SEQUENCE.
  3. "The R gene product of bacteriophage lambda is the murein transglycosylase."
    Bienkowska-Szewczyk K., Lipinska B., Taylor A.
    Mol. Gen. Genet. 184:111-114(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. "Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme."
    Evrard C., Fastrez J., Soumillion P.
    FEBS Lett. 460:442-446(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-31; HIS-48 AND HIS-137.
  5. "Phage lysis: do we have the hole story yet?"
    Young R.
    Curr. Opin. Microbiol. 16:790-797(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes."
    Evrard C., Fastrez J., Declercq J.-P.
    J. Mol. Biol. 276:151-164(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), ACTIVE SITE.
  7. "Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda."
    Di Paolo A., Duval V., Matagne A., Redfield C.
    Biomol. NMR. Assign. 4:111-114(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiENLYS_LAMBD
AccessioniPrimary (citable) accession number: P03706
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 91 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, Direct protein sequencing, 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.