ArticleExtremophiles : life under extreme conditions2006
An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: gene cloning, expression and characterization.
Article in Extremophiles : life under extreme conditions, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- A haloarchaeal VapBC toxin-antitoxin system: regulatory mechanism and role in establishing population heterogeneity to facilitate survival of subpopulations under stress conditions.Applied and environmental microbiology · 2026Article
- Identification and characterization of a novel halolysin from Halostella sp. PRR32 with two C-terminal extensions.Extremophiles : life under extreme conditions · 2025Article
- Identification and biochemical characterization of a novel halolysin from Halorubellus sp. PRR65 with a relatively high temperature activity.World journal of microbiology & biotechnology · 2024Article
- A TrmBL2-like transcription factor mediates the growth phase-dependent expression of halolysin SptA in a concentration-dependent manner inApplied and environmental microbiology · 2024Article
- HtrAs are essential for the survival of the haloarchaeonApplied and environmental microbiology · 2024Article
- Expression, purification, and enzymatic characterization of an extracellular protease from Halococcus salifodinae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review.Bioresources and bioprocessing · 2023Review
- Extracellular proteases from halophiles: diversity and application challenges.Applied microbiology and biotechnology · 2023Review
- Recent advances in the production, properties and applications of haloextremozymes protease and lipase from haloarchaea.World journal of microbiology & biotechnology · 2023Review
- Dissecting the Arginine and Lysine Biosynthetic Pathways and Their Relationship in Haloarchaeon Natrinema gari J7-2 via Endogenous CRISPR-Cas System-Based Genome Editing.Microbiology spectrum · 2023Article
- Hly176B, a low-salt tolerant halolysin from the haloarchaeon Haloarchaeobius sp. FL176.World journal of microbiology & biotechnology · 2023Article
- Simultaneous purification and characterization of detergent-stable, solvent-tolerant haloextremozymes protease and lipase from Haloferax sp. strain GUBF 2.Archives of microbiology · 2022Article
- Sec-Dependent Secretion of Subtilase SptE inApplied and environmental microbiology · 2022Article
- A novel halolysin without C-terminal extension from an extremely halophilic archaeon.Applied microbiology and biotechnology · 2022Article
- Halolysin R4 ofApplied and environmental microbiology · 2021Article
- Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-DegradingFrontiers in microbiology · 2020Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Biotechnological applications of archaeal enzymes from extreme environments.Biological research · 2018Review
- Halolysin SptA, a Serine Protease, Contributes to Growth-Phase Transition of HaloarchaeonFrontiers in microbiology · 2018Article
- Construction of Expression Shuttle Vectors for the HaloarchaeonArchaea (Vancouver, B.C.) · 2017Article
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6 authors.
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Abstract
A gene encoding an extracellular protease, sptA, was cloned from the halophilic archaeon Natrinema sp. J7. It encoded a polypeptide of 565 amino acids containing a putative 49-amino acid signal peptide, a 103-amino acid propeptide, as well as a mature region and C-terminal extension, with a high proportion of acidic amino acid residues. The sptA gene was expressed in Haloferax volcanii WFD11, and the recombinant enzyme could be secreted into the medium as an active mature form. The N-terminal amino acid sequencing and MALDI-TOF mass spectrometry analysis of the purified SptA protease indicated that the 152-amino acid prepropeptide was cleaved and the C-terminal extension was not processed after secretion. The SptA protease was optimally active at 50 degrees C in 2.5 M NaCl at pH 8.0. The NaCl removed enzyme retained 20% of its activity, and 60% of the activity could be restored by reintroducing 2.5 M NaCl into the NaCl removed enzyme. When the twin-arginine motif in the signal peptide of SptA protease was replaced with a twin-lysine motif, the enzyme was not exported from Hfx. volcanii WFD11, suggesting that the SptA protease was a Tat-dependent substrate.
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