ArticleJournal of bacteriology2013
Functional and structural study of the dimeric inner membrane protein SbmA.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
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- Structural and Functional Characteristics of the Proline-Rich Antimicrobial Peptide Minibactenecin from Leukocytes of Domestic Goat Capra hircus.Bulletin of experimental biology and medicine · 2023Article
- Antibiotic synergist OM19r reverses aminoglycoside resistance in multidrug-resistantFrontiers in microbiology · 2023Article
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- Molecular mechanism of antibiotic resistance induced by mono- and twin-chained quaternary ammonium compounds.The Science of the total environment · 2022Article
- Translocation of non-lytic antimicrobial peptides and bacteria penetrating peptides across the inner membrane of the bacterial envelope.Current genetics · 2022Review
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- Cloning and Characterization ofBiomolecules · 2021Article
- The Microbial Toxin Microcin B17: Prospects for the Development of New Antibacterial Agents.Journal of molecular biology · 2019Review
- Discovery and structure of the antimicrobial lasso peptide citrocin.The Journal of biological chemistry · 2019Article
- Combined Antibacterial Effects of Goat Cathelicidins With Different Mechanisms of Action.Frontiers in microbiology · 2018Article
- Modulation of Global Transcriptional Regulatory Networks as a Strategy for Increasing Kanamycin Resistance of the Translational Elongation Factor-G Mutants inG3 (Bethesda, Md.) · 2017Article
- Structural and Functional Basis for Lipid Synergy on the Activity of the Antibacterial Peptide ABC Transporter McjD.The Journal of biological chemistry · 2016Article
- Influence of the yjiL-mdtM Gene Cluster on the Antibacterial Activity of Proline-Rich Antimicrobial Peptides Overcoming Escherichia coli Resistance Induced by the Missing SbmA Transporter System.Antimicrobial agents and chemotherapy · 2015Article
- SCMMTP: identifying and characterizing membrane transport proteins using propensity scores of dipeptides.BMC genomics · 2015Article
- Mechanism of Escherichia coli resistance to Pyrrhocoricin.Antimicrobial agents and chemotherapy · 2014Article
- The C-terminal part of microcin B is crucial for DNA gyrase inhibition and antibiotic uptake by sensitive cells.Journal of bacteriology · 2014Article
- Enteric YaiW is a surface-exposed outer membrane lipoprotein that affects sensitivity to an antimicrobial peptide.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
SbmA protein has been proposed as a dimeric secondary transporter. The protein is involved in the transport of microcins B17 and J25, bleomycin, proline-rich antimicrobial peptides, antisense peptide phosphorodiamidate morpholino oligomers, and peptide nucleic acids into the Escherichia coli cytoplasm. The sbmA homologue is found in a variety of bacteria, though the physiological role of the protein is hitherto unknown. In this work, we carried out a functional and structural analysis to determine which amino acids are critical for the transport properties of SbmA. We created a set of 15 site-directed sbmA mutants in which single conserved amino acids were replaced by glycine residues. Our work demonstrated that strains carrying the site-directed mutants V102G, F219G, and E276G had a null phenotype for SbmA transport functions. In contrast, strains carrying the single point mutants W19G, W53G, F60G, S69G, N155G, R190, L233G, A344G, T255G, N308G, and R385G showed transport capacities indistinguishable from those of strains harboring a wild-type sbmA. The strain carrying the Y116G mutant exhibited mixed phenotypic characteristics. We also demonstrated that those sbmA mutants with severely impaired transport capacity showed a dominant negative phenotype. Electron microscopy data and in silico three-dimensional (3D) homology modeling support the idea that SbmA forms a homodimeric complex, closely resembling the membrane-spanning region of the ATP-binding cassette transporter family. Direct mapping of the sbmA single point mutants on the protein surface allowed us to explain the observed phenotypic differences in transport ability.
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