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Gene Review

EF0799  -  autolysin

Enterococcus faecalis V583

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Disease relevance of EF0799

  • The C-terminal region (cA) of the major autolysin AcmA of Lactococcus lactis contains three highly similar repeated regions of 45 amino acid residues (LysM domains), which are separated by nonhomologous sequences [1].
  • Effect of disruption of a gene encoding an autolysin of Enterococcus faecalis OG1RF [2].
  • Experiments with Streptococcus faecalis whole cells, cell walls, and crude autolysin preparations implicated endogenous autolytic muramidases as the bacterial targets of chitotriose and chitobiose [3].
  • Autolysin activity, as defined by the ability to lyse heat-killed Micrococcus lysodeikticus cells, was absent in TX5127, while this activity was easily detectable in OG1RF [2].
  • The virulence of TX5127 was similar to that of OG1RF in the mouse peritonitis model, indicating that the autolysin of E. faecalis is not important for infection in this model [2].

High impact information on EF0799


Biological context of EF0799

  • The plasmid was found to integrate into the chromosome of OG1RF by a single crossover event, resulting in a disrupted autolysin gene [7].
  • Bacteriolysis induced by the antibiotic can be modulated by addition of EDTA, divalent cations and autolysin activators (trypsin) or inhibitors (cardiolipin), suggesting that topologic regulation of the autolysins is involved in the process [8].

Anatomical context of EF0799


Associations of EF0799 with chemical compounds

  • In addition, inhibitors of protein and RNA synthesis interfere markedly with bacteriolysis, as do ionophores and the ATPase inhibitor DCCD, suggesting the participation of an internal messenger in autolysin activation in the presence of AS-48 [8].

Analytical, diagnostic and therapeutic context of EF0799

  • In addition, isotope labeling and ultrastructural studies were able to show that latent autolysin was concentrated in the newer, septally associated portion of the wall [9].


  1. Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents. Steen, A., Buist, G., Leenhouts, K.J., El Khattabi, M., Grijpstra, F., Zomer, A.L., Venema, G., Kuipers, O.P., Kok, J. J. Biol. Chem. (2003) [Pubmed]
  2. Effect of disruption of a gene encoding an autolysin of Enterococcus faecalis OG1RF. Qin, X., Singh, K.V., Xu, Y., Weinstock, G.M., Murray, B.E. Antimicrob. Agents Chemother. (1998) [Pubmed]
  3. Bactericidal activity of human lysozyme, muramidase-inactive lysozyme, and cationic polypeptides against Streptococcus sanguis and Streptococcus faecalis: inhibition by chitin oligosaccharides. Laible, N.J., Germaine, G.R. Infect. Immun. (1985) [Pubmed]
  4. Processing of streptococcal cell walls by rat macrophages and human monocytes in vitro. Smialowicz, R.J., Schwab, J.H. Infect. Immun. (1977) [Pubmed]
  5. Peptidoglycan O acetylation and autolysin profile of Enterococcus faecalis in the viable but nonculturable state. Pfeffer, J.M., Strating, H., Weadge, J.T., Clarke, A.J. J. Bacteriol. (2006) [Pubmed]
  6. Effects of fatty acids on lysis of Streptococcus faecalis. Carson, D.D., Daneo-Moore, L. J. Bacteriol. (1980) [Pubmed]
  7. Conjugal transfer of plasmid DNA from Escherichia coli to enterococci: a method to make insertion mutations. Teng, F., Murray, B.E., Weinstock, G.M. Plasmid (1998) [Pubmed]
  8. Induction of autolysis in Enterococcus faecalis S-47 by peptide AS-48. Gálvez, A., Valdivia, E., Martínez-Bueno, M., Maqueda, M. J. Appl. Bacteriol. (1990) [Pubmed]
  9. Autolytic formation of protoplasts (autoplasts) of Streptococcus faecalis; location of active and latent autolysin. Joseph, R., Shockman, G.D. J. Bacteriol. (1976) [Pubmed]
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