ArticlePloS one2015
Membrane Topology and Biochemical Characterization of the Escherichia coli BacA Undecaprenyl-Pyrophosphate Phosphatase.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 43 citations in OpenAlex.
- Pardon the interruption: how Und-P sequestration has reshaped our understanding of the bacterial cell envelope.Journal of bacteriology · 2026Review
- Analysis of the regulation of undecaprenyl diphosphate dephosphorylation in Escherichia coli.FEBS open bio · 2025Article
- Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics.Journal of the American Chemical Society · 2024Article
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology.Microbial cell factories · 2024Article
- Repeat-Unit Elongations To Produce Bacterial Complex Long Polysaccharide Chains, an O-Antigen Perspective.EcoSal Plus · 2023Review
- Comparative genomics hints at dispensability of multiple essential genes in two Escherichia coli L-form strains.Bioscience reports · 2023Article
- Recent Advances in Peptidoglycan Synthesis and Regulation in Bacteria.Biomolecules · 2023Review
- The Bacterial Cell Wall: From Lipid II Flipping to Polymerization.Chemical reviews · 2022Review
- Towards discovery of inhibitors of the undecaprenyl-pyrophosphate phosphatase BacA by virtual high-throughput screening.Computational and structural biotechnology journal · 2022Article
- A genetic screen to identify factors affected by undecaprenyl phosphate recycling uncovers novel connections to morphogenesis in Escherichia coli.Molecular microbiology · 2021Article
- Structure, catalysis, and inhibition mechanism of prenyltransferase.IUBMB life · 2021Review
- Minimal exposure of lipid II cycle intermediates triggers cell wall antibiotic resistance.Nature communications · 2019Article
- Coupling of polymerase and carrier lipid phosphatase prevents product inhibition in peptidoglycan synthesis.Cell surface (Amsterdam, Netherlands) · 2018Article
- Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.Nature communications · 2018Article
- Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis.Nature communications · 2018Article
- In situ serial crystallography for rapid de novo membrane protein structure determination.Communications biology · 2018Article
- Depletion of Undecaprenyl Pyrophosphate Phosphatases Disrupts Cell Envelope Biogenesis in Bacillus subtilis.Journal of bacteriology · 2016Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several integral membrane proteins exhibiting undecaprenyl-pyrophosphate (C55-PP) phosphatase activity were previously identified in Escherichia coli that belonged to two distinct protein families: the BacA protein, which accounts for 75% of the C55-PP phosphatase activity detected in E. coli cell membranes, and three members of the PAP2 phosphatidic acid phosphatase family, namely PgpB, YbjG and LpxT. This dephosphorylation step is required to provide the C55-P carrier lipid which plays a central role in the biosynthesis of various cell wall polymers. We here report detailed investigations of the biochemical properties and membrane topology of the BacA protein. Optimal activity conditions were determined and a narrow-range substrate specificity with a clear preference for C55-PP was observed for this enzyme. Alignments of BacA protein sequences revealed two particularly well-conserved regions and several invariant residues whose role in enzyme activity was questioned by using a site-directed mutagenesis approach and complementary in vitro and in vivo activity assays. Three essential residues Glu21, Ser27, and Arg174 were identified, allowing us to propose a catalytic mechanism for this enzyme. The membrane topology of the BacA protein determined here experimentally did not validate previous program-based predicted models. It comprises seven transmembrane segments and contains in particular two large periplasmic loops carrying the highly-conserved active site residues. Our data thus provide evidence that all the different E. coli C55-PP phosphatases identified to date (BacA and PAP2) catalyze the dephosphorylation of C55-PP molecules on the same (outer) side of the plasma membrane.
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