Gene Ontology annotation through association of InterPro records with GO terms.
UniProtKB reviewed entry for pvdT
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UniProt identifies PvdT as the ATP-binding/permease subunit of the PvdRT-OpmQ pyoverdine export system, with ATPase activity and inner-membrane localization.
"This subunit binds PVD and drives"
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PvdT is also implicated in recycling of pyoverdine after ferri-PVD internalization and iron release in the periplasm.
"is also responsible for recycling of PVD after internalization of"
Combined automated GO annotation using multiple IEA methods.
Gene Ontology annotation based on Ensembl/UniProtKB orthology or projection pipelines.
Electronic Gene Ontology annotations created by ARBA machine learning models.
The ABC transporter family efflux pump PvdRT-OpmQ of Pseudomonas putida KT2440: purification and initial characterization.
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Biochemical characterization shows PvdT ATPase activity, stimulation by PvdR, and interaction with pyoverdine.
"We show that PvdT possesses an ATPase activity that is stimulated by the addition of PvdR"
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PvdT and PvdR were purified as the inner-membrane and periplasmic-adapter components of the system, with first direct evidence of pyoverdine interaction.
"purified and characterized the inner membrane component PvdT and the periplasmic adapter protein PvdR"
PvdRT-OpmQ and MdtABC-OpmB efflux systems are involved in pyoverdine secretion in Pseudomonas putida KT2440.
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Genetic evidence links PvdRT-OpmQ to pyoverdine secretion and iron-limited growth.
"Deletion of pvdRT-opmQ leads to reduced amounts of pyoverdine in the medium and decreased growth under iron limitation"
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Expression of the pvdRT-opmQ system is induced by iron limitation, consistent with a role in siderophore-mediated iron acquisition.
"Expression from the respective promoters is stimulated by iron limitation"
Falcon deep research report for pvdT (Q88F88, PP_4210) in Pseudomonas putida KT2440
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PvdT is the inner-membrane ABC (MacB-like) ATPase/permease component of the tripartite PvdRT-OpmQ pyoverdine efflux pump.
"PvdT is the inner-membrane ABC (MacB-like) ATPase/permease component"
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PvdT energizes pyoverdine export by ATP hydrolysis and assembles with the periplasmic adaptor PvdR (and outer-membrane channel OpmQ) into a functional complex.
"energizes export by ATP hydrolysis and forms a functional complex with the periplasmic adaptor"
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Pyoverdine is the cognate substrate/ligand for the PvdT-containing complex, supported by biochemical modulation of ATPase kinetics.
"pyoverdine as the relevant substrate/ligand for the PvdT-containing complex"
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The PvdRT-OpmQ system mediates secretion of both newly synthesized and recycled pyoverdine.
"secretion of newly synthesized and recycled pyoverdine"
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PvdT localizes to the inner membrane as the ABC ATPase/TMD component of the tripartite system spanning inner membrane to periplasm to outer membrane.
"Inner membrane (as the ABC ATPase/TMD component of the tripartite system spanning inner membrane"
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PvdRT-OpmQ contributes substantially but redundantly to pyoverdine export; deletion reduces but does not abolish secretion due to overlapping efflux systems.
"consistent with a major role in export/recycling"