ArticleApplied and environmental microbiology2000
Molecular cloning, sequencing, and expression of omp-40, the gene coding for the major outer membrane protein from the acidophilic bacterium Thiobacillus ferrooxidans.
Article in Applied and environmental microbiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 57 citations in OpenAlex.
- Microbial diversity, metabolic properties, and biotechnological prospects of acid-sulfate soils.World journal of microbiology & biotechnology · 2025Review
- Acidophilic sulphate-reducing bacteria: Diversity, ecophysiology, and applications.Environmental microbiology reports · 2024Review
- Review
- Eurypsychrophilic acidophiles: From (meta)genomes to low-temperature biotechnologies.Frontiers in microbiology · 2023Review
- Leucine-Responsive Regulatory Protein in Acetic Acid Bacteria Is Stable and Functions at a Wide Range of Intracellular pH Levels.Journal of bacteriology · 2021Article
- Integrative Genomics Sheds Light on Evolutionary Forces Shaping the Acidithiobacillia Class Acidophilic Lifestyle.Frontiers in microbiology · 2021Article
- Article
- Microbial response to acid stress: mechanisms and applications.Applied microbiology and biotechnology · 2020Review
- Uncovering the Mechanisms of Halotolerance in the Extremely Acidophilic Members of theFrontiers in microbiology · 2019Article
- Acidithiobacillus ferrooxidans and its potential application.Extremophiles : life under extreme conditions · 2018Review
- Survival and Energy Producing Strategies of Alkane Degraders Under Extreme Conditions and Their Biotechnological Potential.Frontiers in microbiology · 2018Review
- Microbial copper resistance: importance in biohydrometallurgy.Microbial biotechnology · 2017Review
- The Ecology of Acidophilic Microorganisms in the Corroding Concrete Sewer Environment.Frontiers in microbiology · 2017Review
- Cytoplasmic CopZ-Like Protein and Periplasmic Rusticyanin and AcoP Proteins as Possible Copper Resistance Determinants in Acidithiobacillus ferrooxidans ATCC 23270.Applied and environmental microbiology · 2016Article
- System-level understanding of the potential acid-tolerance components of Acidithiobacillus thiooxidans ZJJN-3 under extreme acid stress.Extremophiles : life under extreme conditions · 2015Article
- Response of Acidithiobacillus caldus toward suboptimal pH conditions.Extremophiles : life under extreme conditions · 2013Article
- Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans.Extremophiles : life under extreme conditions · 2011Article
- Molecular aspects of bacterial pH sensing and homeostasis.Nature reviews. Microbiology · 2011Review
- Acidithiobacillus thiooxidans secretome containing a newly described lipoprotein Licanantase enhances chalcopyrite bioleaching rate.Applied microbiology and biotechnology · 2011Article
- Selection and evaluation of reference genes for improved interrogation of microbial transcriptomes: case study with the extremophile Acidithiobacillus ferrooxidans.BMC molecular biology · 2009Article
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2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thiobacillus ferrooxidans is one of the chemolithoautotrophic bacteria important in industrial biomining operations. Some of the surface components of this microorganism are probably involved in adaptation to their acidic environment and in bacterium-mineral interactions. We have isolated and characterized omp40, the gene coding for the major outer membrane protein from T. ferrooxidans. The deduced amino acid sequence of the Omp40 protein has 382 amino acids and a calculated molecular weight of 40,095.7. Omp40 forms an oligomeric structure of about 120 kDa that dissociates into the monomer (40 kDa) by heating in the presence of sodium dodecyl sulfate. The degree of identity of Omp40 amino acid sequence to porins from enterobacteria was only 22%. Nevertheless, multiple alignments of this sequence with those from several OmpC porins showed several important features conserved in the T. ferrooxidans surface protein, such as the approximate locations of 16 transmembrane beta strands, eight loops, including a large external L3 loop, and eight turns which allowed us to propose a putative 16-stranded beta-barrel porin structure for the protein. These results together with the previously known capacity of Omp40 to form ion channels in planar lipid bilayers strongly support its role as a porin in this chemolithoautotrophic acidophilic microorganism. Some characteristics of the Omp40 protein, such as the presence of a putative L3 loop with an estimated isoelectric point of 7.21 allow us to speculate that this can be the result of an adaptation of the acidophilic T. ferrooxidans to prevent free movement of protons across its outer membrane.
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