J. Bacteriol., Feb 1996, 1227-1231, Vol 178, No. 4
Copyright © 1996, American Society for Microbiology
C Sauvage, T Franza and D Expert
Laboratoire de Pathologie Vegetale, Institut National de la Recherche Agronomique, Paris, France.
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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