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The TonB‐dependent ferrichrome receptor FcuA of Yersinia enterocolitica : evidence against a strict co‐evolution of receptor structure and substrate specificity
Author(s) -
Koebnik Ralf,
Hantke Klaus,
Braun Volkmar
Publication year - 1993
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.1365-2958.1993.tb01130.x
Subject(s) - ferrichrome , biology , yersinia enterocolitica , peptide sequence , escherichia coli , mutant , colicin , microbiology and biotechnology , bacterial outer membrane , biochemistry , gene , bacteria , genetics
Summary A Yersinia enterocolitica receptor mutant was isolated which is impaired in ferrichrome uptake. The receptor‐encoding gene fcuA was cloned in Escherichia coli K‐12. A fcuA mutant of Y. enterocolitica could be complemented by the cloned DNA fragment. The FcuA‐encoding region was sequenced and an open reading frame encoding 758 amino acids including a signal sequence of 36 amino acids was found. FcuA shared 34.6% amino acid sequence homology with FatA, the anguibactin receptor of Vibrio anguillarum , but only 20.6% homology with FhuA, the ferrichrome receptor of E. coli Since the structure of anguibactin differs strongly from that of ferrichrome there seems to be no co‐evolution of receptor structure and substrate specificity. The ferrichrome receptors FcuA from Y. enterocolitica and FhuA from E. coli had slightly different substrate specificities. In contrast to FhuA from E. coli , FcuA from Y. enterocolitica was more stereoselective and failed to transport enantio ferrichrome. Three additional ferrichrome receptors were cloned from Pantoea aggiomerans (formerly Erwinia herbicola), Salmonella paratyphi B and Salmonella typhimurium. Their substrate specificity was similar but not identical.