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M. Dalla Costa, P. E. Reynolds, H. A. Souza, D. C. Souza, M. F. Palepou, and N. Woodford, Antimicrob. Agents Chemother. 44:3444-3446, 2000). A G\n                    <jats:sub>184<\/jats:sub>\n                    S mutation adjacent to the serine involved in the binding of\n                    <jats:sc>d<\/jats:sc>\n                    -Ala1 in the\n                    <jats:sc>d<\/jats:sc>\n                    -alanine:\n                    <jats:sc>d<\/jats:sc>\n                    -alanine ligase (Ddl) led to production of an impaired Ddl and accounts for the lack of\n                    <jats:sc>d<\/jats:sc>\n                    -alanyl-\n                    <jats:sc>d<\/jats:sc>\n                    -alanine-containing peptidoglycan precursors. The sequence of the\n                    <jats:italic>vanD<\/jats:italic>\n                    gene cluster revealed eight open reading frames. The organization of this operon, assigned to a chromosomal location, was similar to those in other VanD type strains. The distal part encoded the VanH\n                    <jats:sub>D<\/jats:sub>\n                    dehydrogenase, the VanD ligase, and the VanX\n                    <jats:sub>D<\/jats:sub>\n                    dipeptidase, which were homologous to the corresponding proteins in VanD-type strains. Upstream from the structural genes for these proteins was the\n                    <jats:italic>\n                      vanY\n                      <jats:sub>D<\/jats:sub>\n                    <\/jats:italic>\n                    gene; a frameshift mutation in this gene resulted in premature termination of the encoded protein and accounted for the lack of penicillin-susceptible\n                    <jats:sc>d<\/jats:sc>\n                    ,\n                    <jats:sc>d<\/jats:sc>\n                    -carboxypeptidase activity. Analysis of the translated sequence downstream from the stop codon, but in a different reading frame because of the frameshift mutation, indicated homology with penicillin binding proteins (PBPs) with a high degree of identity with VanY\n                    <jats:sub>D<\/jats:sub>\n                    from VanD-type strains. The 5\u2032 end of the gene cluster contained the\n                    <jats:italic>\n                      vanR\n                      <jats:sub>D<\/jats:sub>\n                    <\/jats:italic>\n                    <jats:italic>\n                      -vanS\n                      <jats:sub>D<\/jats:sub>\n                    <\/jats:italic>\n                    genes for a putative two-component regulatory system. Insertion of IS\n                    <jats:italic>Efa4<\/jats:italic>\n                    in the\n                    <jats:italic>\n                      vanS\n                      <jats:sub>D<\/jats:sub>\n                    <\/jats:italic>\n                    gene led to constitutive expression of vancomycin resistance. This new insertion belonged to the IS\n                    <jats:italic>605<\/jats:italic>\n                    family and was composed of two open reading frames encoding putative transposases of two unrelated insertion sequence elements, IS\n                    <jats:italic>200<\/jats:italic>\n                    and IS\n                    <jats:italic>1341<\/jats:italic>\n                    .\n                  <\/jats:p>","DOI":"10.1128\/aac.47.1.7-18.2003","type":"journal-article","created":{"date-parts":[[2002,12,23]],"date-time":"2002-12-23T23:39:08Z","timestamp":1040686748000},"page":"7-18","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":66,"title":["VanD-Type Vancomycin-Resistant\n                    <i>Enterococcus faecium<\/i>\n                    10\/96A"],"prefix":"10.1128","volume":"47","author":[{"given":"Florence","family":"Depardieu","sequence":"first","affiliation":[{"name":"Unite\u0301 des Agents Antibacte\u0301riens, Institut Pasteur, 75724 Paris, Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter E.","family":"Reynolds","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Cambridge, Cambridge CB21QW, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrice","family":"Courvalin","sequence":"additional","affiliation":[{"name":"Unite\u0301 des Agents Antibacte\u0301riens, Institut Pasteur, 75724 Paris, Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a122817"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/25.17.3389"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.01114.x"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1099\/13500872-145-8-1849"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.179.1.97-106.1997"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(94)00851-I"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.43.8.1875"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1996.00617.x"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.38.9.1899"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.36.4.867"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.174.8.2582-2591.1992"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.175.1.117-127.1993"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/0966-842X(96)10063-9"},{"key":"e_1_3_2_15_2","unstructured":"Ausubel F. 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