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P03706 (ENLYS_LAMBD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endolysin

EC=4.2.2.n2
Alternative name(s):
Lysis protein
Lysozyme
Muramidase
Transglycosylase
Gene names
Name:R
OrganismEnterobacteria phage lambda (Bacteriophage lambda) [Reference proteome]
Taxonomic identifier10710 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Subunit structure

Monomer.

Subcellular location

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

Sequence similarities

Belongs to the glycosyl hydrolase 24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Endolysin
PRO_0000218108

Sites

Active site191 Ref.6

Experimental info

Mutagenesis311H → D: No effect on lytic activity. Ref.4
Mutagenesis311H → N: No effect on lytic activity; when associated with N-137. Ref.4
Mutagenesis481H → N: 97% loss of lytic activity. Ref.4
Mutagenesis1371H → N: No effect on lytic activity; when associated with N-31. Ref.4
Sequence conflict741Missing AA sequence Ref.2

Secondary structure

......................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03706 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 94F8E9A512EAA03E

FASTA15817,825
        10         20         30         40         50         60 
MVEINNQRKA FLDMLAWSEG TDNGRQKTRN HGYDVIVGGE LFTDYSDHPR KLVTLNPKLK 

        70         80         90        100        110        120 
STGAGRYQLL SRWWDAYRKQ LGLKDFSPKS QDAVALQQIK ERGALPMIDR GDIRQAIDRC 

       130        140        150 
SNIWASLPGA GYGQFEHKAD SLIAKFKEAG GTVREIDV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of bacteriophage lambda DNA."
Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.
J. Mol. Biol. 162:729-773(1982) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02459 Genomic DNA. Translation: AAA96598.1.
PIREYBPL. B04333.
RefSeqNP_040645.1. NC_001416.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AM7X-ray2.30A/B/C1-158[»]
1D9UX-ray2.60A/B1-154[»]
3D3DX-ray2.60A/B1-154[»]
ProteinModelPortalP03706.
SMRP03706. Positions 1-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03706. 1 interaction.

Protein family/group databases

CAZyGH104. Glycoside Hydrolase Family 104.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703480.

Family and domain databases

InterProIPR002196. Glyco_hydro_24.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00959. Phage_lysozyme. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03706.

Entry information

Entry nameENLYS_LAMBD
AccessionPrimary (citable) accession number: P03706
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries