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Two of the clustered genes,\n            <jats:italic>bceD<\/jats:italic>\n            and\n            <jats:italic>bceF<\/jats:italic>\n            , code for two proteins homologous to phosphotyrosine phosphatases and tyrosine kinases, respectively. We show experimental evidence indicating that BceF is phosphorylated on tyrosine and that the conserved lysine residue present at position 563 in the Walker A ATP-binding motif is required for this autophosphorylation. It was also proved that BceD is capable of dephosphorylating the phosphorylated BceF. Using the artificial substrate\n            <jats:italic>p<\/jats:italic>\n            -nitrophenyl phosphate (PNPP), BceD exhibited a\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            of 8.8 \u03bcmol of PNPP min\n            <jats:sup>\u22121<\/jats:sup>\n            mg\n            <jats:sup>\u22121<\/jats:sup>\n            and a\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            of 3.7 mM PNPP at 30\u00b0C. The disruption of\n            <jats:italic>bceF<\/jats:italic>\n            resulted in the abolishment of cepacian accumulation in the culture medium, but 75% of the parental strain's EPS production yield was still registered for the\n            <jats:italic>bceD<\/jats:italic>\n            mutant. The exopolysaccharide produced by the\n            <jats:italic>bceD<\/jats:italic>\n            mutant led to less viscous solutions and exhibited the same degree of acetylation as the wild-type cepacian, suggesting a lower molecular mass for this mutant biopolymer. The size of the biofilm produced in vitro by\n            <jats:italic>bceD<\/jats:italic>\n            and\n            <jats:italic>bceF<\/jats:italic>\n            mutant strains is smaller than the size of the biofilm formed by the parental strain, and this phenotype was confirmed by complementation assays, indicating that BceD and BceF play a role in the establishment of biofilms of maximal size.\n          <\/jats:p>","DOI":"10.1128\/aem.01450-06","type":"journal-article","created":{"date-parts":[[2006,11,18]],"date-time":"2006-11-18T08:56:44Z","timestamp":1163840204000},"page":"524-534","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":53,"title":["Functional Analysis of\n            <i>Burkholderia cepacia<\/i>\n            Genes\n            <i>bceD<\/i>\n            and\n            <i>bceF<\/i>\n            , Encoding a Phosphotyrosine Phosphatase and a Tyrosine Autokinase, Respectively: Role in Exopolysaccharide Biosynthesis and Biofilm Formation"],"prefix":"10.1128","volume":"73","author":[{"given":"Ana S.","family":"Ferreira","sequence":"first","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Centro de Engenharia Biolo\u0301gica e Qui\u0301mica, Instituto Superior Te\u0301cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal"}]},{"given":"Jorge H.","family":"Leita\u0303o","sequence":"additional","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Centro de Engenharia Biolo\u0301gica e Qui\u0301mica, Instituto Superior Te\u0301cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal"}]},{"given":"Si\u0301lvia A.","family":"Sousa","sequence":"additional","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Centro de Engenharia Biolo\u0301gica e Qui\u0301mica, Instituto Superior Te\u0301cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal"}]},{"given":"Ana M.","family":"Cosme","sequence":"additional","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Centro de Engenharia Biolo\u0301gica e Qui\u0301mica, Instituto Superior Te\u0301cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal"}]},{"given":"Isabel","family":"Sa\u0301-Correia","sequence":"additional","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Centro de Engenharia Biolo\u0301gica e Qui\u0301mica, Instituto Superior Te\u0301cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal"}]},{"given":"Leonilde M.","family":"Moreira","sequence":"additional","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Centro de Engenharia Biolo\u0301gica e Qui\u0301mica, Instituto Superior Te\u0301cnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/25.17.3389"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1995.tb02292.x"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.185.20.6057-6066.2003"},{"key":"e_1_3_2_5_2","first-page":"104","volume":"6","year":"1984","unstructured":"Beutler, H. 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