Flagellar hook-basal body complex protein FliE

No Pfam abstract.

InterPro entry IPR001624

Four genes from the major Bacillus subtilis chemotaxis locus have been shown to encode proteins that are similar to the Salmonella typhimurium FlgB, FlgC, FlgG and FliF proteins; a further gene product is similar to the Escherichia coli FliE protein PUBMED:1905667. All of these proteins are thought to form part of the hook-basal body complex of the bacterial flagella PUBMED:1905667. The FlgB, FlgC and FlgG proteins are components of the proximal and distal rods; FliF forms the M-ring that anchors the rod assembly to the membrane; but the role of FliE has not yet been determined PUBMED:1905667. The similarity between the proteins in these two organisms suggests that the structures of the M-ring and the rod may be similar PUBMED:1905667. Nevertheless, some differences in size and amino acid composition between some of the homologues suggest the basal body proteins may be organised slightly differently within B. subtilis PUBMED:1905667.

From gel electrophoresis and autoradiography of 35S-labelled S. typhimurium hook-basal body complexes and the deduced number of sulphur-containing residues in FliE, the stoichiometry of the protein in the hook-basal body complex has been estimated to be about nine subunits PUBMED:1551848. FliE does not undergo cleavage of a signal peptide, nor does it show any similarity to the axial components like the rod or hook proteins, which are thought to be exported by the flagellum-specific export pathway PUBMED:1551848. On this evidence, it has been suggested that FliE may be in the vicinity of the MS ring, perhaps acting as an adaptor protein between ring and rod substructures PUBMED:1551848.

Gene Ontology

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HMM information