Processing of the major autolysin of E. faecalis, AtlA, by the zinc-metalloprotease, GelE, impacts AtlA septal localization and cell separation.

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Stinemetz, Emily K.; Gao, Peng; Pinkston, Kenneth L.; Montealegre, Maria Camila; Murray, Barbara E.; Harvey, Barrett R.;
(2017)
  • Publisher: Public Library of Science (PLoS)
  • Journal: PLoS ONE,volume 12,issue 10 (issn: 1932-6203, eissn: 1932-6203)
  • Publisher copyright policies & self-archiving
  • Related identifiers: doi: 10.1371/journal.pone.0186706, pmc: PMC5648223
  • Subject: Macromolecules | Enterococcus Faecalis | Microbial Pathogens | Research Article | Bacteria | Pathology and Laboratory Medicine | Peptidoglycans | Immunoassays | Enzymes | Polymer Chemistry | Materials by Structure | Cell Processes | Chemical Reactions | Physical Sciences | Pathogens | Proteins | Enzyme-Linked Immunoassays | Polymers | Light Microscopy | Chemistry | Biology and Life Sciences | Materials Science | Research and Analysis Methods | Microbiology | Recombinant Proteins | Hydrolases | Medicine | Bacterial Pathogens | Immunologic Techniques | Enzymology | Medical Microbiology | Q | R | Cell Biology | Enterococcus | Biochemistry | Science | Organisms | Microscopy | Medicine and Health Sciences | Hydrolysis | Cell Cycle and Cell Division

AtlA is the major peptidoglycan hydrolase of Enterococcus faecalis involved in cell division and cellular autolysis. The secreted zinc metalloprotease, gelatinase (GelE), has been identified as an important regulator of cellular function through post-translational modif... View more
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