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P03706

- ENLYS_LAMBD

UniProt

P03706 - ENLYS_LAMBD

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Protein

Endolysin

Gene

R

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed - 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

  1. carbon-oxygen lyase activity, acting on polysaccharides Source: UniProtKB-EC
  2. lysozyme activity Source: InterPro

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
  5. viral release from host cell Source: UniProtKB-KW
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: 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

  1. host cell cytoplasm Source: UniProtKB-KW
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 – 1813
Beta strandi21 – 266
Turni31 – 344
Beta strandi53 – 564
Beta strandi59 – 613
Turni65 – 684
Helixi71 – 8111
Helixi88 – 10114
Helixi105 – 1106
Helixi113 – 1208
Turni121 – 1233
Beta strandi132 – 1343
Helixi135 – 14814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 [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 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02459 Genomic DNA. Translation: AAA96598.1.
PIRiB04333. EYBPL.
RefSeqiNP_040645.1. NC_001416.1.

Genome annotation databases

GeneIDi2703480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02459 Genomic DNA. Translation: AAA96598.1 .
PIRi B04333. EYBPL.
RefSeqi NP_040645.1. NC_001416.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AM7 X-ray 2.30 A/B/C 1-158 [» ]
1D9U X-ray 2.60 A/B 1-154 [» ]
3D3D X-ray 2.60 A/B 1-154 [» ]
ProteinModelPortali P03706.
SMRi P03706. Positions 1-154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03706. 1 interaction.

Protein family/group databases

CAZyi GH104. Glycoside Hydrolase Family 104.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703480.

Miscellaneous databases

EvolutionaryTracei P03706.

Family and domain databases

InterProi IPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00959. Phage_lysozyme. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 88 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