{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T23:57:21Z","timestamp":1791158241115,"version":"4.1.0"},"reference-count":59,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2007,4,1]],"date-time":"2007-04-01T00:00:00Z","timestamp":1175385600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2007,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            WecA is an integral membrane protein that initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide (LPS) by catalyzing the transfer of\n            <jats:italic>N<\/jats:italic>\n            -acetylglucosamine (GlcNAc)-1-phosphate onto undecaprenyl phosphate (Und-P) to form Und-P-P-GlcNAc. WecA belongs to a large family of eukaryotic and prokaryotic prenyl sugar transferases. Conserved aspartic acids in putative cytoplasmic loops 2 (Asp90 and Asp91) and 3 (Asp156 and Asp159) were targeted for replacement mutagenesis with either glutamic acid or asparagine. We examined the ability of each mutant protein to complement O-antigen LPS synthesis in a\n            <jats:italic>wecA<\/jats:italic>\n            -deficient strain and also determined the steady-state kinetic parameters of the mutant proteins in an in vitro transfer assay. Apparent\n            <jats:italic>\n              K\n              <jats:sub>m<\/jats:sub>\n            <\/jats:italic>\n            and\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            values for UDP-GlcNAc, Mg\n            <jats:sup>2+<\/jats:sup>\n            , and Mn\n            <jats:sup>2+<\/jats:sup>\n            suggest that Asp156 is required for catalysis, while Asp91 appears to interact preferentially with Mg\n            <jats:sup>2+<\/jats:sup>\n            , possibly playing a role in orienting the substrates. Topological analysis using the substituted cysteine accessibility method demonstrated the cytosolic location of Asp90, Asp91, and Asp156 and provided a more refined overall topological map of WecA. Also, we show that cells expressing a WecA derivative C terminally fused with the green fluorescent protein exhibited a punctate distribution of fluorescence on the bacterial surface, suggesting that WecA localizes to discrete regions in the bacterial plasma membrane.\n          <\/jats:p>","DOI":"10.1128\/jb.01905-06","type":"journal-article","created":{"date-parts":[[2007,1,20]],"date-time":"2007-01-20T01:25:29Z","timestamp":1169256329000},"page":"2618-2628","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":137,"title":["Functional Characterization and Membrane Topology of\n            <i>Escherichia coli<\/i>\n            WecA, a Sugar-Phosphate Transferase Initiating the Biosynthesis of Enterobacterial Common Antigen and O-Antigen Lipopolysaccharide"],"prefix":"10.1128","volume":"189","author":[{"given":"Jason","family":"Lehrer","sequence":"first","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Departments of Microbiology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen A.","family":"Vigeant","sequence":"additional","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Departments of Microbiology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura D.","family":"Tatar","sequence":"additional","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Departments of Microbiology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel A.","family":"Valvano","sequence":"additional","affiliation":[{"name":"Infectious Diseases Research Group, Siebens-Drake Medical Research Institute, Departments of Microbiology and Immunology"},{"name":"Medicine, University of Western Ontario, London, Ontario N6A 5C1, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.176.22.7079-7084.1994"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1006\/jmbi.1999.2837","volume":"289","year":"1999","unstructured":"Allingham, J. S., P. A. Pribil, and D. B. Haniford. 1999. All three residues of the Tn10 transposase DDE catalytic triad function in divalent metal ion binding. J. Mol. Biol. 289 : 1195-1206.","journal-title":"J. Mol. Biol."},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"3015","DOI":"10.1099\/00221287-147-11-3015","volume":"147","year":"2001","unstructured":"Amer, A. O., and M. A. Valvano. 2001. Conserved amino acid residues found in a predicted cytosolic domain of WecA (UDP-N-acetyl glucosamine:undecaprenol-phosphate N-acetylglucosamine-1-phosphate transferase) are implicated in the recognition of UDP-N-acetylglucosamine. Microbiology 147 : 3015-3025.","journal-title":"Microbiology"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1099\/00221287-148-2-571","volume":"148","year":"2002","unstructured":"Amer, A. O., and M. A. Valvano. 2002. 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