Endolysin

Details

Name

Endolysin

Synonyms

• 4.2.2.n2
• Lysis protein
• Lysozyme
• Muramidase
• Transglycosylase

Gene Name

R

Organism

Enterobacteria phage lambda

Amino acid sequence

>lcl|BSEQ0016637|Endolysin
MVEINNQRKAFLDMLAWSEGTDNGRQKTRNHGYDVIVGGELFTDYSDHPRKLVTLNPKLK
STGAGRYQLLSRWWDAYRKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRC
SNIWASLPGAGYGQFEHKADSLIAKFKEAGGTVREIDV

Number of residues

158

Molecular Weight

17825.045

Theoretical pI

9.66

GO Classification

Functions

carbon-oxygen lyase activity, acting on polysaccharides / lysozyme activity

Processes

cell wall macromolecule catabolic process / cytolysis / defense response to bacterium / peptidoglycan catabolic process / viral release from host cell

Components

host cell cytoplasm

General Function

Lysozyme activity

Specific 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.

Pfam Domain Function

• Phage_lysozyme (PF00959)

Transmembrane Regions

Not Available

Cellular Location

Host cytoplasm

Gene sequence

>lcl|BSEQ0016638|Endolysin (R)
ATGGTAGAAATCAATAATCAACGTAAGGCGTTCCTCGATATGCTGGCGTGGTCGGAGGGA
ACTGATAACGGACGTCAGAAAACCAGAAATCATGGTTATGACGTCATTGTAGGCGGAGAG
CTATTTACTGATTACTCCGATCACCCTCGCAAACTTGTCACGCTAAACCCAAAACTCAAA
TCAACAGGCGCCGGACGCTACCAGCTTCTTTCCCGTTGGTGGGATGCCTACCGCAAGCAG
CTTGGCCTGAAAGACTTCTCTCCGAAAAGTCAGGACGCTGTGGCATTGCAGCAGATTAAG
GAGCGTGGCGCTTTACCTATGATTGATCGTGGTGATATCCGTCAGGCAATCGACCGTTGC
AGCAATATCTGGGCTTCACTGCCGGGCGCTGGTTATGGTCAGTTCGAGCATAAGGCTGAC
AGCCTGATTGCAAAATTCAAAGAAGCGGGCGGAACGGTCAGAGAGATTGATGTATGA

Chromosome Location

Not Available

Locus

Not Available

External Identifiers

Resource	Link
UniProtKB ID	P03706
UniProtKB Entry Name	ENLYS_LAMBD
GenBank Protein ID	215163
GenBank Gene ID	J02459

General References

1. Sanger F, Coulson AR, Hong GF, Hill DF, Petersen GB: Nucleotide sequence of bacteriophage lambda DNA. J Mol Biol. 1982 Dec 25;162(4):729-73. [Article]
2. Bienkowska-Szewczyk K, Lipinska B, Taylor A: The R gene product of bacteriophage lambda is the murein transglycosylase. Mol Gen Genet. 1981;184(1):111-4. [Article]
3. Evrard C, Fastrez J, Soumillion P: Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme. FEBS Lett. 1999 Nov 5;460(3):442-6. [Article]
4. Young R: Phage lysis: do we have the hole story yet? Curr Opin Microbiol. 2013 Dec;16(6):790-7. doi: 10.1016/j.mib.2013.08.008. Epub 2013 Oct 8. [Article]
5. Evrard C, Fastrez J, Declercq JP: Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes. J Mol Biol. 1998 Feb 13;276(1):151-64. [Article]
6. Di Paolo A, Duval V, Matagne A, Redfield C: Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. Biomol NMR Assign. 2010 Apr;4(1):111-4. doi: 10.1007/s12104-010-9219-8. Epub 2010 Mar 20. [Article]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB04206	7-Aza-L-tryptophan	experimental	unknown		Details