title: The rfb genes in Azotobacter vinelandii are arranged in a rfbFGC gene cluster: a significant deviation to the arrangement of the rfb genes in Enterobacteriaceae.
abstract: We report the identification of rfbF and rfbC located adjacent to the previously identified rfbG (Gavini et. al. Biochem. Biophys. Res. Commun. 1997, 240, 153-161) from the non-symbiotic, non-pathogenic soil bacterium Azotobacter vinelandii. The rfbF open reading frame encodes a putative polypeptide of 256 amino acids. This polypeptide shares a homology of 74% with the RfbF of Synechocystis sp. and a 70% homology with the AscA of Yersinia pseudotuberculosis which function as alpha-D-glucose-1-phosphate cytidylyltransferases in the biosynthesis of the O-antigen. The rfbC encodes a putative polypeptide of 186 amino acids. It shows strongest homology to the RfbC of Synechocystis sp. (64%) and Salmonella typhimurium (40%). RfbC functions as a dTDP-4-Dehydrorhamnose 3,5-Epimerase. The genes identified here have a low G + C content (approximately 56%) as compared to the A. vinelandii chromosome (approximately 63%) which is characteristic of the rfb clusters identified in other bacteria and may be indicative of the acquisition of the rfb genes by interspecific gene transfer. Despite the high level of sequence conservation, the organization of the rfb genes in A. vinelandii deviates from the arrangement of the most thoroughly studied rfb gene clusters of Enterobacteriaceae.
authors.affiliation: Department of Biological Sciences, Bowling Green State University, Ohio 43403, USA.
authors.forename: B S
authors.initials: BS
authors.lastname: Hausman
authors.forename: J A
authors.initials: JA
authors.lastname: Williamson
authors.forename: R P
authors.initials: RP
authors.lastname: Schreiner
authors.forename: L
authors.initials: L
authors.lastname: Pulakat
authors.forename: N
authors.initials: N
authors.lastname: Gavini
mesh_terms: D000595:Amino Acid Sequence; D000942:Antigens, Bacterial; D016948:Azotobacter vinelandii / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D002238:Carbohydrate Epimerases / Q000737:chemistry; D003001:Cloning, Molecular; D004755:Enterobacteriaceae / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics; D008969:Molecular Sequence Data; D019081:O Antigens / Q000096:biosynthesis; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
chemical_list: D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D019081:O Antigens; C110120:RfbF protein, Campylobacter coli; C079397:rfb protein, Bacteria; D002238:Carbohydrate Epimerases; C088100:TDP-deoxyglucose epimerase