ArticleThe Journal of biological chemistry2011
Characterization of a Listeria monocytogenes Ca(2+) pump: a SERCA-type ATPase with only one Ca(2+)-binding site.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 49 citations in OpenAlex.
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- Dephosphorylation and ion binding in prokaryotic calcium transport.Science advances · 2024Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Characterization of CaBiochimica et biophysica acta. Biomembranes · 2023Article
- Structure and ion-release mechanism of PeLife · 2021Article
- Transmembrane Cu(I) P-type ATPase pumps are electrogenic uniporters.Dalton transactions (Cambridge, England : 2003) · 2020Article
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- Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
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- Transcriptional activation by MafR, a global regulator of Enterococcus faecalis.Scientific reports · 2019Article
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- Engineering a Prototypic P-type ATPase Listeria monocytogenes Ca(2+)-ATPase 1 for Single-Molecule FRET Studies.Bioconjugate chemistry · 2016Article
- A sulfur-based transport pathway in Cu+-ATPases.EMBO reports · 2015Article
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- Calcium homeostasis in Pseudomonas aeruginosa requires multiple transporters and modulates swarming motility.Cell calcium · 2013Article
- Characterization of the PIB-Type ATPases present in Thermus thermophilus.Journal of bacteriology · 2012Article
- Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have characterized a putative Ca(2+)-ATPase from the pathogenic bacterium Listeria monocytogenes with the locus tag lmo0841. The purified and detergent-solubilized protein, which we have named Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1), performs a Ca(2+)-dependent ATP hydrolysis and actively transports Ca(2+) after reconstitution in dioleoylphosphatidyl-choline vesicles. Despite a high sequence similarity to the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) and plasma membrane Ca(2+)-ATPase (PMCA), LMCA1 exhibits important biochemical differences such as a low Ca(2+) affinity (K(0.5) ∼80 μm) and a high pH optimum (pH ∼9). Mutational studies indicate that the unusually high pH optimum can be partially ascribed to the presence of an arginine residue (Arg-795), corresponding in sequence alignments to the Glu-908 position at Ca(2+) binding site I of rabbit SERCA1a, but probably with an exposed position in LMCA1. The arginine is characteristic of a large group of putative bacterial Ca(2+)-ATPases. Moreover, we demonstrate that H(+) is countertransported with a transport stoichiometry of 1 Ca(2+) out and 1 H(+) in per ATP hydrolyzed. The ATPase may serve an important function by removing Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH.
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