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Ferrioxamine uptake in Yersinia enterocolitica : characterization of the receptor protein FoxA
Author(s) -
Báumler Andreas J.,
Hantke Klaus
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb00852.x
Subject(s) - biology , yersinia enterocolitica , open reading frame , ferrichrome , peptide sequence , amino acid , genetics , escherichia coli , gene , bacterial outer membrane , bacteria
Summary 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 75768 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.