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

ABSTRACT: 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.

SUBMITTER: Willemsen PT

PROVIDER: S-EPMC179347 | biostudies-other | 1997 Aug

REPOSITORIES: biostudies-other

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

Willemsen P T PT Vulto I I Boxem M M de Graaff J J

Journal of bacteriology 19970801 15

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 meningiti ...[more]

PMID: 9244288

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