title: Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site.
abstract: BACKGROUND
  Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, here renamed LcpA, previously associated with the regulation of the expression of the low-affinity PBP5 and β-lactam resistance, has been characterized.
  
  
  RESULTS
  LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of secondary cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae.
  
  
  CONCLUSIONS
  LcpA belongs to the LytR-CpsA-Psr family. Its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.
authors.affiliation: Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium.
authors.forename: Maxime
authors.initials: M
authors.lastname: Maréchal
authors.affiliation: Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium.
authors.forename: Ana
authors.initials: A
authors.lastname: Amoroso
authors.affiliation: University Grenoble Alpes, IBS, Grenoble, F-38044, France.|CNRS, IBS, Grenoble, F-38044, France.|CEA, IBS, Grenoble, F-38044, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Morlot
authors.affiliation: University Grenoble Alpes, IBS, Grenoble, F-38044, France.|CNRS, IBS, Grenoble, F-38044, France.|CEA, IBS, Grenoble, F-38044, France.
authors.forename: Thierry
authors.initials: T
authors.lastname: Vernet
authors.affiliation: Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium.
authors.forename: Jacques
authors.initials: J
authors.lastname: Coyette
authors.affiliation: Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium. bjoris@ulg.ac.be.
authors.forename: Bernard
authors.identifier: http://orcid.org/0000-0003-0407-9302
authors.initials: B
authors.lastname: Joris
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D000070076:Enterococcus hirae / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D010457:Peptidoglycan / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism; D060066:Protein Interaction Maps; D011994:Recombinant Proteins; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D018440:beta-Lactam Resistance
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial; D010457:Peptidoglycan; C080374:Psr protein, Enterococcus hirae; D011994:Recombinant Proteins; D012097:Repressor Proteins; D010770:Phosphotransferases
keywords: Bacterial division; Cell wall; Enterococcus; LytR-CpsA-Psr; Peptidoglycan