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Microbiology 141 (1995), 2253-2260
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microbiology, Vol 141, 2253-2260, Copyright © 1995 by Society for General Microbiology

ARTICLES

Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: characterization of the fruB gene

V de Crecy-Lagard, M Binet and A Danchin
Unite de Regulation de l'Expression genetique, Institut Pasteur, Paris, France.

In the plant pathogen Xanthomonas campestris pv. campestris, fructose is transported by a specific phosphotransferase system (PTS). This PTS involves a multiphosphoryl transfer protein (MTP) encoded by the fruB gene, which was cloned and sequenced. fruB is part of a transcriptional unit together with the fruK gene, coding for 1-phosphofructokinase, which is located upstream from the fruA gene, coding for the fructose- specific permease (EIIB'BCFru). The amino acid sequence of the X. campestris MTP deduced from the fruB sequence shared 46% identical residues with an MTP identified in Rhodobacter capsulatus. The X. campestris MTP (837 amino acid residues) consists of three moieties: a fructose-specific enzyme-IIA-like N-terminal moiety (residues 1-148), followed by an HPr-like moiety (161-251) and an enzyme-I-like C- terminal moiety (274-837). The three domains are separated by two flexible hinge regions rich in proline and alanine residues. The construction of a fruB mutant confirmed the role of the MTP in fructose transport and phosphorylation in X. campestris.


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