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J. Bacteriol., Aug 1997, 4949-4952, Vol 179, No. 15
Copyright © 1997, American Society for Microbiology

Characterization of a periplasmic protein involved in iron utilization of Actinobacillus actinomycetemcomitans

PT Willemsen, I Vulto, M Boxem and J de Graaff
Department of Oral Microbiology, Academic Centre for Dentistry Amsterdam, The Netherlands. PTJ.Willemsen.omb.acta@med.vu.nl

The periodontopathic bacterium Actinobacillus actinomycetemcomitans possesses a 35-kDa periplasmic iron-repressible protein. Its regulation is mediated by the Fur protein, as was inferred from the Fur-binding consensus sequence at the -35 position of the gene for the 35-kDa protein and from the relaxed expression of the gene in a mutant with an altered Fur-binding sequence. The 35-kDa protein, designated AfuA, has strong homology to HitA and FbpA of Haemophilus influenzae and Neisseria meningitidis, respectively, which serve as periplasmic iron transport proteins.


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