Lysozyme

NameLysozyme
Synonyms
  • 3.2.1.17
  • Lysis protein
  • Lysozyme
  • Muramidase
Gene NameE
OrganismEnterobacteria phage T4
Amino acid sequence
>lcl|BSEQ0016364|Endolysin
MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITK
DEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL
Number of residuesNone
Molecular Weight18691.385
Theoretical pI10.08
GO Classification
Functions
  • lysozyme activity
Processes
  • defense response to bacterium
  • cytolysis
  • viral release from host cell
  • peptidoglycan catabolic process
  • cell wall macromolecule catabolic process
Components
  • host cell cytoplasm
General FunctionLysozyme activity
Specific FunctionEndolysin with lysozyme 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP00720
UniProtKB Entry Name
Cellular LocationHost cytoplasm
Gene sequence
>lcl|BSEQ0016365|Endolysin (E)
ATGAATATATTTGAAATGTTACGTATAGATGAACGTCTTAGACTTAAAATCTATAAAGAC
ACAGAAGGCTATTACACTATTGGCATCGGTCATTTGCTTACAAAAAGTCCATCACTTAAT
GCTGCTAAATCTGAATTAGATAAAGCTATTGGGCGTAATTGCAATGGTGTAATTACAAAA
GATGAGGCTGAAAAACTCTTTAATCAGGATGTTGATGCTGCTGTTCGCGGAATTCTGAGA
AATGCTAAATTAAAACCGGTTTATGATTCTCTTGATGCGGTTCGTCGCTGTGCATTGATT
AATATGGTTTTCCAAATGGGAGAAACCGGTGTGGCAGGATTTACTAACTCTTTACGTATG
CTTCAACAAAAACGCTGGGATGAAGCAGCAGTTAACTTAGCTAAAAGTATATGGTATAAT
CAAACACCTAATCGCGCAAAACGAGTCATTACAACGTTTAGAACTGGCACTTGGGACGCG
TATAAAAATCTATAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Inouye M, Imada M, Tsugita A: The amino acid sequence of T4 phage lysozyme. IV. Dilute acid hydrolysis and the order of tryptic peptides. J Biol Chem. 1970 Jul 25;245(14):3479-84. [5470817 ]
  2. Owen JE, Schultz DW, Taylor A, Smith GR: Nucleotide sequence of the lysozyme gene of bacteriophage T4. Analysis of mutations involving repeated sequences. J Mol Biol. 1983 Apr 5;165(2):229-48. [6302287 ]
  3. Valerie K, Stevens J, Lynch M, Henderson EE, de Riel JK: Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of bacteriophage T4. Nucleic Acids Res. 1986 Nov 11;14(21):8637-54. [3024113 ]
  4. Miller ES, Kutter E, Mosig G, Arisaka F, Kunisawa T, Ruger W: Bacteriophage T4 genome. Microbiol Mol Biol Rev. 2003 Mar;67(1):86-156, table of contents. [12626685 ]
  5. Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R: Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. [22389108 ]
  6. Matthews BW, Remington SJ: The three dimensional structure of the lysozyme from bacteriophage T4. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4178-82. [4530293 ]
  7. Weaver LH, Matthews BW: Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. J Mol Biol. 1987 Jan 5;193(1):189-99. [3586019 ]
  8. Remington SJ, Eyck LF, Matthews BW: Atomic coordinates for T4 phage lysozyme. Biochem Biophys Res Commun. 1977 Mar 21;75(2):265-70. [322662 ]
  9. Matsumura M, Becktel WJ, Matthews BW: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature. 1988 Aug 4;334(6181):406-10. [3405287 ]
  10. Faber HR, Matthews BW: A mutant T4 lysozyme displays five different crystal conformations. Nature. 1990 Nov 15;348(6298):263-6. [2234094 ]
  11. Eriksson AE, Baase WA, Wozniak JA, Matthews BW: A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature. 1992 Jan 23;355(6358):371-3. [1731252 ]
  12. McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW: Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme. Biochemistry. 1990 Jul 10;29(27):6341-62. [2207079 ]

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