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Literature summary for 2.1.1.294 extracted from

  • Clarke, B.R.; Greenfield, L.K.; Bouwman, C.; Whitfield, C.
    Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway (2009), J. Biol. Chem., 284, 30662-30672.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the WbdD protein is tethered to the membrane via a C-terminal region containing amphipathic helices located between residues 601 and 669 Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Escherichia coli O9a
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Synonyms

Synonyms Comment Organism
WbdD ambiguous Escherichia coli

General Information

General Information Comment Organism
malfunction membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity Escherichia coli
physiological function WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction Escherichia coli