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
- Functionscarbon-oxygen lyase activity, acting on polysaccharides / lysozyme activityProcessescell wall macromolecule catabolic process / cytolysis / defense response to bacterium / peptidoglycan catabolic process / viral release from host cellComponentshost 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
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]