Analysis of the Erwinia chrysanthemi ferrichrysobactin receptor gene: resemblance to the Escherichia coli fepA-fes bidirectional promoter region and homology with hydroxamate receptors.
The fct cbsCEBA operon from the Erwinia chrysanthemi 3937 chrysobactin-dependent iron assimilation system codes for transport and biosynthetic functions. The sequence of the fct outer membrane receptor gene was determined. The fct promoter region displays a strong resemblance to the Escherichia coli bidirectional intercistronic region controlling the expression of the fepA-entD and fes-entF operons. An apparent Fur-binding site was shown to confer iron regulation on an fct::lac fusion expressed on a low-copy-number plasmid in a Fur-proficient E. coli strain. The fct gene consists of an open reading frame encoding a 735-amino-acid polypeptide with a signal sequence of 38 residues. The Fct protein has 36% sequence homology with the E. coli ferrichrome receptor FhuA and the Yersinia enterocolitica ferrioxamine receptor FoxA. On the basis of secondary-structure predictions and these homologies, we propose a two-dimensional folding model for Fct.
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Laboratoire de Pathologie Végétale, Institut National de la Recherche Agronomique, Paris, France.
Franza
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Expert
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D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics*; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D002265:Carboxylic Ester Hydrolases / Q000235:genetics; D002352:Carrier Proteins / Q000235:genetics; D016974:Dickeya chrysanthemi / Q000235:genetics*; D004151:Dipeptides / Q000378:metabolism; D029968:Escherichia coli Proteins; D005290:Ferric Compounds / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D007501:Iron / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D009876:Operon; D011401:Promoter Regions, Genetic; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface / Q000235:genetics*; D011991:Receptors, Virus / Q000235:genetics; D012097:Repressor Proteins / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D017262:Siderophores / Q000378:metabolism; D014158:Transcription, Genetic
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D004151:Dipeptides; D029968:Escherichia coli Proteins; D005290:Ferric Compounds; C050900:FhuA protein, E coli; C489524:FoxA protein, bacteria; C489523:FoxB protein, E coli; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D011991:Receptors, Virus; D012097:Repressor Proteins; D017262:Siderophores; C029489:enterobactin receptor; C068477:ferric uptake regulating proteins, bacterial; C098063:ferrichysobactin receptor, Pectobacterium chrysanthemi; C057616:tonB protein, Bacteria; C489181:tonB protein, E coli; C058543:chrysobactin; D007501:Iron; D002265:Carboxylic Ester Hydrolases