Bacterial flagellar diversity in the post-genomic era.
Flagellar biosynthesis has been studied most thoroughly in laboratory strains of Escherichia coli and Salmonella enterica. However, genome sequencing has uncovered flagellar loci in distantly related bacteria. We have used homology searches to determine how far the E. coli/S. enterica paradigm can be generalised to other flagellar systems. Numerous previously unrecognized homologues of flagellar components were discovered, including novel FlgM, FlgN, FliK and FliO homologues. Homology was found between the FliK proteins and a molecular ruler, YscP, from a virulence-associated type-III secretion system. Also described is a new family of flagellar proteins, the FlhX proteins, which resemble the cytoplasmic domain of FlhB.
Pallen
Mark J
MJ
Bacterial Pathogenesis and Genomics Unit, Division of Immunity and Infection, Medical School, University of Birmingham, Birmingham, UK B15 2TT. m.pallen@bham.ac.uk
Penn
Charles W
CW
Chaudhuri
Roy R
RR
D000595:Amino Acid Sequence; D001419:Bacteria / Q000235:genetics* / Q000648:ultrastructure; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001692:Biological Transport; D019295:Computational Biology; D005407:Flagella / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D005798:Genes, Bacterial; D016680:Genome, Bacterial; D018832:Molecular Chaperones / Q000378:metabolism; D008969:Molecular Sequence Data; D009068:Movement; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D018832:Molecular Chaperones