The N-terminal region of the Escherichia coli WecA (Rfe) protein, containing three predicted transmembrane helices, is required for function but not for membrane insertion.
The correct site for translation initiation for Escherichia coli WecA (Rfe), presumably involved in catalyzing the transfer of N-acetylglucosamine 1-phosphate to undecaprenylphosphate, was determined by using its FLAG-tagged derivatives. The N-terminal region containing three predicted transmembrane helices was found to be necessary for function but not for membrane localization of this protein.
Amer
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Department of Microbiology, University of Western Ontario, London, Ontario N6A 5C1, Canada.
Valvano
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D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D002384:Catalysis; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli; D006602:Hexosyltransferases; D008969:Molecular Sequence Data; D009842:Oligopeptides; D010455:Peptides / Q000378:metabolism; D014176:Protein Biosynthesis; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D009842:Oligopeptides; D010455:Peptides; C026146:N-acetylglucosamine-1-phosphate; C085706:FLAG peptide; D006602:Hexosyltransferases; C122139:RgpG protein, Streptococcus mutans; D000117:Acetylglucosamine