Ferrioxamine uptake in Yersinia enterocolitica: Characterization of the receptor protein FoxA

Andreas J Baumler, Klaus Hantke

Research output: Contribution to journalArticlepeer-review

82 Scopus citations

Abstract

The gene for the high-affinity outer membrane ferrioxamine receptor FoxA of Yersinia enterocolitica was cloned in Escherichia coli K-12. A foxA mutant of Yersinia could be complemented by the cloned DNA fragment. The FoxA encoding region was sequenced and an open reading frame encoding 710 amino acids, including a signal sequence of 26 amino acids, was deduced. The mature FoxA protein consisted of 684 amino acids and had a molecular mass of 75 768 Da. FoxA shared 33% amino acid sequence homology with FhuA, the ferrichrome receptor of Escherichia coli. Based on the homologies with FhuA and other TonB-dependent receptors a topological model of FoxA is presented.

Original languageEnglish (US)
Pages (from-to)1309-1321
Number of pages13
JournalMolecular Microbiology
Volume6
Issue number10
StatePublished - May 1992
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

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