Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
MgtE is a dual-function protein in Pseudomonas aeruginosa.
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P. aeruginosa MgtE transports Mg2+ and regulates cytotoxicity, and Mg2+-binding sites of the connecting helix, identified from a model based on the T. thermophilus structure, are needed to couple the two.
"We demonstrated both magnesium transport and cytotoxicity-regulating functions, and showed that magnesium-binding sites in the connecting helix region of MgtE are vital in coupling these two functions."
The Pseudomonas aeruginosa magnesium transporter MgtE inhibits transcription of the type III secretion system.
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mgtE mutation increases T3SS transcription; transport-defective mgtE variants still complement the cytotoxicity phenotype.
"mgtE variants that were defective for magnesium transport could still complement the cytotoxicity effect"
Pseudomonas aeruginosa Magnesium Transporter MgtE Inhibits Type III Secretion System Gene Expression by Stimulating rsmYZ Transcription.
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mgtE expression acts through GacAS to increase rsmY/rsmZ and inhibit exsA translation.
"We now demonstrate that mgtE expression acts through the GacAS two-component system to activate rsmY and rsmZ transcription."
Crystal structure of the MgtE Mg2+ transporter.
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T. thermophilus MgtE is a homodimer with Mg2+ bound in the pore and at cytosolic sensor sites between the connecting helices and other domains.
"A solvent-accessible pore nearly traverses the transmembrane domains, with one potential Mg2+ bound to the conserved Asp 432 within the pore."
Mg(2+)-dependent gating of bacterial MgtE channel underlies Mg(2+) homeostasis.
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T. thermophilus MgtE is a Mg2+-selective channel gated by cytosolic Mg2+.
"Here, we showed that MgtE is a highly Mg(2+)-selective channel gated by Mg(2+)"
UniProt entry Q9I544 (Q9I544_PSEAE)
PAINT node PTN000227060 composition and Mg2+-site conservation in PA0913