Pacing across the membrane: the novel PACE family of efflux pumps is widespread in Gram-negative pathogens

The proteobacterial antimicrobial compound efflux (PACE) family of transport proteins was only recently described. PACE family transport proteins can confer resistance to a range of biocides used as disinfectants and antiseptics, and are encoded by many important Gram-negative human pathogens. Howev...

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Published in	Research in microbiology Vol. 169; no. 7-8; pp. 450 - 454
Main Authors	Hassan, Karl A., Liu, Qi, Elbourne, Liam D.H., Ahmad, Irshad, Sharples, David, Naidu, Varsha, Chan, Chak Lam, Li, Liping, Harborne, Steven P.D., Pokhrel, Alaska, Postis, Vincent L.G., Goldman, Adrian, Henderson, Peter J.F., Paulsen, Ian T.
Format	Journal Article
Language	English
Published	France Elsevier Masson SAS 01.09.2018 Elsevier
Subjects	amino acid motifs amino acid sequences animal pathogens anti-infective agents Antimicrobial resistance antiseptics Bacterial transmembrane pair domain biocides disinfectants drug resistance Efflux genes germplasm conservation Gram-negative bacteria Gram-negative pathogen interspersed repetitive sequences Membrane transport PACE transporters Efflux Antimicrobial resistance Bacterial transmembrane pair domain Gram-negative pathogen Membrane transport PACE
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Abstract	The proteobacterial antimicrobial compound efflux (PACE) family of transport proteins was only recently described. PACE family transport proteins can confer resistance to a range of biocides used as disinfectants and antiseptics, and are encoded by many important Gram-negative human pathogens. However, we are only just beginning to appreciate the range of functions and the mechanism(s) of transport operating in these proteins. Genes encoding PACE family proteins are typically conserved in the core genomes of bacterial species rather than on recently acquired mobile genetic elements, suggesting that they confer important core functions in addition to biocide resistance. Three-dimensional structural information is not yet available for PACE family proteins. However, PACE proteins have several very highly conserved amino acid sequence motifs that are likely to be important for substrate transport. PACE proteins also display strong amino acid sequence conservation between their N and C-terminal halves, suggesting that they evolved by duplication of an ancestral protein comprised of two transmembrane helices. In light of their drug resistance functions in Gram-negative pathogens, PACE proteins should be the subject of detailed future investigation.
AbstractList	The proteobacterial antimicrobial compound efflux (PACE) family of transport proteins was only recently described. PACE family transport proteins can confer resistance to a range of biocides used as disinfectants and antiseptics, and are encoded by many important Gram-negative human pathogens. However, we are only just beginning to appreciate the range of functions and the mechanism(s) of transport operating in these proteins. Genes encoding PACE family proteins are typically conserved in the core genomes of bacterial species rather than on recently acquired mobile genetic elements, suggesting that they confer important core functions in addition to biocide resistance. Three-dimensional structural information is not yet available for PACE family proteins. However, PACE proteins have several very highly conserved amino acid sequence motifs that are likely to be important for substrate transport. PACE proteins also display strong amino acid sequence conservation between their N and C-terminal halves, suggesting that they evolved by duplication of an ancestral protein comprised of two transmembrane helices. In light of their drug resistance functions in Gram-negative pathogens, PACE proteins should be the subject of detailed future investigation.The proteobacterial antimicrobial compound efflux (PACE) family of transport proteins was only recently described. PACE family transport proteins can confer resistance to a range of biocides used as disinfectants and antiseptics, and are encoded by many important Gram-negative human pathogens. However, we are only just beginning to appreciate the range of functions and the mechanism(s) of transport operating in these proteins. Genes encoding PACE family proteins are typically conserved in the core genomes of bacterial species rather than on recently acquired mobile genetic elements, suggesting that they confer important core functions in addition to biocide resistance. Three-dimensional structural information is not yet available for PACE family proteins. However, PACE proteins have several very highly conserved amino acid sequence motifs that are likely to be important for substrate transport. PACE proteins also display strong amino acid sequence conservation between their N and C-terminal halves, suggesting that they evolved by duplication of an ancestral protein comprised of two transmembrane helices. In light of their drug resistance functions in Gram-negative pathogens, PACE proteins should be the subject of detailed future investigation. The proteobacterial antimicrobial compound efflux (PACE) family of transport proteins was only recently described. PACE family transport proteins can confer resistance to a range of biocides used as disinfectants and antiseptics, and are encoded by many important Gram-negative human pathogens. However, we are only just beginning to appreciate the range of functions and the mechanism(s) of transport operating in these proteins. Genes encoding PACE family proteins are typically conserved in the core genomes of bacterial species rather than on recently acquired mobile genetic elements, suggesting that they confer important core functions in addition to biocide resistance. Three-dimensional structural information is not yet available for PACE family proteins. However, PACE proteins have several very highly conserved amino acid sequence motifs that are likely to be important for substrate transport. PACE proteins also display strong amino acid sequence conservation between their N— and C-terminal halves, suggesting that they evolved by duplication of an ancestral protein comprised of two transmembrane helices. In light of their drug resistance functions in Gram-negative pathogens, PACE proteins should be the subject of detailed future investigation.
Author	Harborne, Steven P.D. Pokhrel, Alaska Li, Liping Naidu, Varsha Henderson, Peter J.F. Paulsen, Ian T. Liu, Qi Postis, Vincent L.G. Chan, Chak Lam Ahmad, Irshad Sharples, David Hassan, Karl A. Goldman, Adrian Elbourne, Liam D.H.
AuthorAffiliation	a School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, Australia c Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia b School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK d Biomedicine Research Group, Faculty of Health and Social Sciences, Leeds Beckett University, Leeds, UK e Division of Biochemistry, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland
AuthorAffiliation_xml	– name: a School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, Australia – name: c Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia – name: b School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – name: d Biomedicine Research Group, Faculty of Health and Social Sciences, Leeds Beckett University, Leeds, UK – name: e Division of Biochemistry, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland
Author_xml	– sequence: 1 givenname: Karl A. surname: Hassan fullname: Hassan, Karl A. email: Karl.Hassan@newcastle.edu.au organization: School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW, Australia – sequence: 2 givenname: Qi surname: Liu fullname: Liu, Qi organization: Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia – sequence: 3 givenname: Liam D.H. surname: Elbourne fullname: Elbourne, Liam D.H. organization: Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia – sequence: 4 givenname: Irshad surname: Ahmad fullname: Ahmad, Irshad organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 5 givenname: David surname: Sharples fullname: Sharples, David organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 6 givenname: Varsha surname: Naidu fullname: Naidu, Varsha organization: Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia – sequence: 7 givenname: Chak Lam surname: Chan fullname: Chan, Chak Lam organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 8 givenname: Liping surname: Li fullname: Li, Liping organization: Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia – sequence: 9 givenname: Steven P.D. surname: Harborne fullname: Harborne, Steven P.D. organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 10 givenname: Alaska surname: Pokhrel fullname: Pokhrel, Alaska organization: Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia – sequence: 11 givenname: Vincent L.G. surname: Postis fullname: Postis, Vincent L.G. organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 12 givenname: Adrian surname: Goldman fullname: Goldman, Adrian organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 13 givenname: Peter J.F. surname: Henderson fullname: Henderson, Peter J.F. organization: School of BioMedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK – sequence: 14 givenname: Ian T. surname: Paulsen fullname: Paulsen, Ian T. organization: Department of Chemistry and Biomolecular Science, Macquarie University, North Ryde, NSW, Australia
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/29409983$$D View this record in MEDLINE/PubMed
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Keywords	Efflux Antimicrobial resistance Bacterial transmembrane pair domain Gram-negative pathogen Membrane transport PACE
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Snippet	The proteobacterial antimicrobial compound efflux (PACE) family of transport proteins was only recently described. PACE family transport proteins can confer...
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SubjectTerms	amino acid motifs amino acid sequences animal pathogens anti-infective agents Antimicrobial resistance antiseptics Bacterial transmembrane pair domain biocides disinfectants drug resistance Efflux genes germplasm conservation Gram-negative bacteria Gram-negative pathogen interspersed repetitive sequences Membrane transport PACE transporters
Title	Pacing across the membrane: the novel PACE family of efflux pumps is widespread in Gram-negative pathogens
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