Literature DB >> 10559160

Characterization of a periplasmic ATP-binding cassette iron import system of Brachyspira (Serpulina) hyodysenteriae.

D Dugourd1, C Martin, C R Rioux, M Jacques, J Harel.   

Abstract

The nucleotide sequence of the pathogenic spirochete Brachyspira hyodysenteriae bit (for "Brachyspira iron transport") genomic region has been determined. The bit region is likely to encode an iron ATP-binding cassette transport system with some homology to those encountered in gram-negative bacteria. Six open reading frames oriented in the same direction and physically linked have been identified. This system possesses a protein containing ATP-binding motifs (BitD), two hydrophobic cytoplasmic membrane permeases (BitE and BitF), and at least three lipoproteins (BitA, BitB, and BitC) with homology to iron periplasmic binding proteins. These periplasmic binding proteins exhibit lipoprotein features. They are labeled by [(3)H]palmitate when tested in recombinant Escherichia coli, and their signal peptides are typical for substrates of the type II secretory peptidase. The FURTA system and Congo red assay indicate that BitB and BitC are involved in iron binding. The Bit system is detected only in B. hyodysenteriae and is absent from B. innocens and B. pilosicoli.

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Year:  1999        PMID: 10559160      PMCID: PMC94169     

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  64 in total

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Journal:  Infect Immun       Date:  1979-09       Impact factor: 3.441

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  8 in total

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8.  The Exposed Proteomes of Brachyspira hyodysenteriae and B. pilosicoli.

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  8 in total

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