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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)DescriptionActionsGraphical viewLength
Active sitei191 Publication1

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]
Proteomesi
  • UP000001711 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)DescriptionActionsGraphical viewLength
Mutagenesisi31H → D: No effect on lytic activity. 1 Publication1
Mutagenesisi31H → N: No effect on lytic activity; when associated with N-137. 1 Publication1
Mutagenesisi48H → N: 97% loss of lytic activity. 1 Publication1
Mutagenesisi137H → N: No effect on lytic activity; when associated with N-31. 1 Publication1

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002181081 – 158EndolysinAdd BLAST158

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP03706. 1 interactor.

Structurei

Secondary structure

1158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 18Combined sources13
Beta strandi21 – 26Combined sources6
Turni31 – 34Combined sources4
Beta strandi53 – 56Combined sources4
Beta strandi59 – 61Combined sources3
Turni65 – 68Combined sources4
Helixi71 – 81Combined sources11
Helixi88 – 101Combined sources14
Helixi105 – 110Combined sources6
Helixi113 – 120Combined sources8
Turni121 – 123Combined sources3
Beta strandi132 – 134Combined sources3
Helixi135 – 148Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AM7X-ray2.30A/B/C1-158[»]
1D9UX-ray2.60A/B1-154[»]
3D3DX-ray2.60A/B1-154[»]
ProteinModelPortaliP03706.
SMRiP03706.
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)DescriptionActionsGraphical viewLength
Sequence conflicti74Missing AA sequence (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AM7X-ray2.30A/B/C1-158[»]
1D9UX-ray2.60A/B1-154[»]
3D3DX-ray2.60A/B1-154[»]
ProteinModelPortaliP03706.
SMRiP03706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03706. 1 interactor.

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.

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...

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: November 30, 2016
This is version 97 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

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 one 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.