Bacillus cereus efflux protein BC3310 - : a multidrug transporter of the unknown major facilitator family, UMF-2

Jasmin K. Kroeger; Karl Hassan; Aniko Vörös; Roger Simm; Massoud Saidijam; Kim E. Bettaney; Andreas Bechthold; Ian T. Paulsen; Peter J F Henderson; Anne Brit Kolstø

doi:10.3389/fmicb.2015.01063

Bacillus cereus efflux protein BC3310 - : a multidrug transporter of the unknown major facilitator family, UMF-2

Jasmin K. Kroeger, Karl Hassan, Aniko Vörös, Roger Simm, Massoud Saidijam, Kim E. Bettaney, Andreas Bechthold, Ian T. Paulsen, Peter J F Henderson, Anne Brit Kolstø^*

^*Corresponding author for this work

Macquarie University BioFocus Research Centre

Research output: Contribution to journal › Article › peer-review

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Abstract

Phylogenetic classification divides the major facilitator superfamily (MFS) into 82 families, including 25 families that are comprised of transporters with no characterized functions. This study describes functional data for BC3310 from Bacillus cereus ATCC 14579, a member of the "unknown major facilitator family-2" (UMF-2). BC3310 was shown to be a multidrug efflux pump conferring resistance to ethidium bromide, SDS and silver nitrate when heterologously expressed in Escherichia coli DH5a ΔacrAB. A conserved aspartate residue (D105) in putative transmembrane helix 4 was identified, which was essential for the energy dependent ethidium bromide efflux by BC3310. Transport proteins of the MFS comprise specific sequence motifs. Sequence analysis of UMF-2 proteins revealed that they carry a variant of the MFS motif A, which may be used as a marker to distinguish easily between this family and other MFS proteins. Genes orthologous to bc3310 are highly conserved within the B. cereus group of organisms and thus belong to the core genome, suggesting an important conserved functional role in the normal physiology of these bacteria.

Original language	English
Article number	1063
Number of pages	12
Journal	Frontiers in Microbiology
Volume	6
DOIs	https://doi.org/10.3389/fmicb.2015.01063
Publication status	Published - 2015

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Copyright the Author(s) 2015. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

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title = "Bacillus cereus efflux protein BC3310 - : a multidrug transporter of the unknown major facilitator family, UMF-2",

abstract = "Phylogenetic classification divides the major facilitator superfamily (MFS) into 82 families, including 25 families that are comprised of transporters with no characterized functions. This study describes functional data for BC3310 from Bacillus cereus ATCC 14579, a member of the {"}unknown major facilitator family-2{"} (UMF-2). BC3310 was shown to be a multidrug efflux pump conferring resistance to ethidium bromide, SDS and silver nitrate when heterologously expressed in Escherichia coli DH5a ΔacrAB. A conserved aspartate residue (D105) in putative transmembrane helix 4 was identified, which was essential for the energy dependent ethidium bromide efflux by BC3310. Transport proteins of the MFS comprise specific sequence motifs. Sequence analysis of UMF-2 proteins revealed that they carry a variant of the MFS motif A, which may be used as a marker to distinguish easily between this family and other MFS proteins. Genes orthologous to bc3310 are highly conserved within the B. cereus group of organisms and thus belong to the core genome, suggesting an important conserved functional role in the normal physiology of these bacteria.",

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note = "Copyright the Author(s) 2015. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher. ",

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doi = "10.3389/fmicb.2015.01063",

language = "English",

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T2 - a multidrug transporter of the unknown major facilitator family, UMF-2

AU - Kroeger, Jasmin K.

AU - Hassan, Karl

AU - Vörös, Aniko

AU - Simm, Roger

AU - Saidijam, Massoud

AU - Bettaney, Kim E.

AU - Bechthold, Andreas

AU - Paulsen, Ian T.

AU - Henderson, Peter J F

AU - Kolstø, Anne Brit

N1 - Copyright the Author(s) 2015. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

PY - 2015

Y1 - 2015

N2 - Phylogenetic classification divides the major facilitator superfamily (MFS) into 82 families, including 25 families that are comprised of transporters with no characterized functions. This study describes functional data for BC3310 from Bacillus cereus ATCC 14579, a member of the "unknown major facilitator family-2" (UMF-2). BC3310 was shown to be a multidrug efflux pump conferring resistance to ethidium bromide, SDS and silver nitrate when heterologously expressed in Escherichia coli DH5a ΔacrAB. A conserved aspartate residue (D105) in putative transmembrane helix 4 was identified, which was essential for the energy dependent ethidium bromide efflux by BC3310. Transport proteins of the MFS comprise specific sequence motifs. Sequence analysis of UMF-2 proteins revealed that they carry a variant of the MFS motif A, which may be used as a marker to distinguish easily between this family and other MFS proteins. Genes orthologous to bc3310 are highly conserved within the B. cereus group of organisms and thus belong to the core genome, suggesting an important conserved functional role in the normal physiology of these bacteria.

AB - Phylogenetic classification divides the major facilitator superfamily (MFS) into 82 families, including 25 families that are comprised of transporters with no characterized functions. This study describes functional data for BC3310 from Bacillus cereus ATCC 14579, a member of the "unknown major facilitator family-2" (UMF-2). BC3310 was shown to be a multidrug efflux pump conferring resistance to ethidium bromide, SDS and silver nitrate when heterologously expressed in Escherichia coli DH5a ΔacrAB. A conserved aspartate residue (D105) in putative transmembrane helix 4 was identified, which was essential for the energy dependent ethidium bromide efflux by BC3310. Transport proteins of the MFS comprise specific sequence motifs. Sequence analysis of UMF-2 proteins revealed that they carry a variant of the MFS motif A, which may be used as a marker to distinguish easily between this family and other MFS proteins. Genes orthologous to bc3310 are highly conserved within the B. cereus group of organisms and thus belong to the core genome, suggesting an important conserved functional role in the normal physiology of these bacteria.

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JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

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Bacillus cereus efflux protein BC3310 - : a multidrug transporter of the unknown major facilitator family, UMF-2

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