Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.181 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 PubMedView publication on EuropePMC
Search for more literature for 2.7.1.181

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
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli O9a
-
-
-

Synonyms

Synonyms Comment Organism
WbdD
-
 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