The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus subtilis

This work was supported by Fundagao para a Ciencia e a Tecnologia (FCT/MCTES http://www.fct.pt/index.phtml.pt) [PEst-OE/BIA/U10457/2011 to Centro de Recursos Microbiologicos (CREM); UID/Multi/04378/2013 to Unidade de Ciencias Biomoleculares Aplicadas (UCIBIO); fellowship SFRH/BD/73039/2010 to M.J.F.]. Lia Godinho constructed pLG31, Grac E a Susete constructed pGS1 and strain IQB622, Liliana Brito constructed pLB1 and strain IQB623, and Joana Lima constructed pJL1. Lu o A s Jaime Mota, Adriano O. Henriques, and Mariana G. Pinho provided the antibodies used for immunoblotting. This work was supported by Fundacao para a Ciencia e a Tecnologia (FCT/MCTES) [PEst-OE/BIA/UI0457/2011 to Centro de Recursos Microbiologicos (CREM); UID/Multi/04378/2013 to Unidade de Ciencias Biomoleculares Aplicadas (UCIBIO); fellowship SFRH/BD/73039/2010 to M.J.F.].Carbohydrates from plant cell walls are often found as heteropolysaccharides intertwined with each other. For competitive advantage against other microorganisms, and ability to fully exploit available carbon and energy sources, Bacillus subtilis possesses a high number of proteins dedicated to the uptake of mono- and oligosaccharides. Here, we characterize transporter complexes, belonging to the ATP-binding cassette (ABC) superfamily, involved in the uptake of oligosaccharides commonly found in pectin. The uptake of these carbohydrates is shown to be MsmX-dependent, assigning a key role in pectin mobilization for MsmX, a multipurpose ATPase serving several distinct ABC-type I sugar importers. Muta-genesis analysis of the transmembrane domains of the AraNPQ MsmX-dependent importer revealed putative residues for MsmX interaction. Interestingly however, although MsmX is shown to be essential for energizing various ABC transporters we found that a second B. subtilis ATPase, YurJ, is able to complement its function when placed in trans at a different locus of the chromosome.publishersversionpublishe