Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
Global topology analysis of the Escherichia coli inner membrane proteome.
The conserved dipole in transmembrane helix 5 of KdpB in the Escherichia coli KdpFABC P-type ATPase is crucial for coupling and the electrogenic K+-translocation step.
The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone.
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KdpB is the ATP-hydrolysing subunit that defines KdpFABC as a type IA P-type ATPase.
"On the basis of the biochemical properties of the ATP-hydrolyzing subunit KdpB, the transport complex is classified as type IA P-type ATPase."
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KdpC interacts with the KdpB nucleotide-binding loop in an ATP-dependent manner.
"the KdpC subunit was shown to interact with the nucleotide-binding loop of KdpB in an ATP-dependent manner around the ATP-binding pocket"
The K+-translocating Kdp-ATPase from Escherichia coli. Purification, enzymatic properties and production of complex- and subunit-specific antisera.
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Purified Kdp-ATPase is a high-affinity K+-uptake ATPase using Mg-ATP.
"The Kdp system from Escherichia coli is a derepressible high-affinity K+-uptake ATPase."
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Anti-KdpB antibodies inhibit membrane-bound and purified ATPase activity.
"the anti-KdpABC and anti-KdpB sera impaired ATPase activity in the membrane-bound as well as in the purified state of the enzyme"
Crystal structure of the potassium-importing KdpFABC membrane complex.
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ATP energy is harnessed by KdpB while K+ moves through KdpA.
"the energy of ATP is harnessed by KdpB"
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K+ in KdpA should trigger Asp307 phosphorylation of KdpB.
"the presence or absence of K+ in KdpA should initiate autophosphorylation of Asp307 in KdpB"
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Ser162 phosphorylation of KdpB inversely correlates with, and inhibits, ATPase activity.
"the inverse correlation between the relative levels of Ser162 phosphorylation and ATPase activity supports the inhibitory nature of this modification"
Cryo-EM structures of KdpFABC suggest a K(+) transport mechanism via two inter-subunit half-channels.
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ATP hydrolysis is carried out by KdpB.
"While ATP hydrolysis is accomplished by the P-type ATPase subunit KdpB"
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K+ translocation runs via two inter-subunit half-channels, integrating KdpB in transport.
"integrating KdpB directly in the transport process"
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Ser162 is phosphorylated in both E1 and E2 cryo-EM states.
"Ser162 (TGES; A domain of KdpB) appears to be phosphorylated in both states"
Structural basis for potassium transport in prokaryotes by KdpFABC.
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KdpB harnesses ATP energy to drive uphill K+ transport.
"KdpB, on the other hand, harnesses the energy of ATP to drive transport of K + against a concentration gradient"
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ATP hydrolysis is coupled to K+ transfer between KdpB sites and release to the cytoplasm.
"Our structures suggest a mechanism where ATP hydrolysis is coupled to K+ transfer between alternative sites in KdpB, ultimately reaching a low-affinity site where a water-filled pathway allows release of K+ to the cytoplasm."
Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli.
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KdpA, KdpB and KdpC are inner membrane proteins.
"have been identified and found to be located in the inner membrane"
Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum.
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KdpB, the phosphorylated subunit, is homologous to SERCA Ca2+-ATPase.
"Regions of the predicted amino acid sequence of KdpB, the phosphorylated protein of the system, are homologous to regions of the Ca2+-ATPase of rabbit sarcoplasmic reticulum."
Genetic evidence for two sequentially occupied K+ binding sites in the Kdp transport ATPase.
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Energy coupling is mediated by KdpB, a different subunit from the transporting KdpA.
"Energy coupling in Kdp, mediated by the KdpB subunit, is performed by a different subunit from the one that mediates transport."
ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli.
Structure and function of the Kdp-ATPase of Escherichia coli.
UniProtKB P03960 (KDPB_ECOLI) record
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KdpB is responsible for energy coupling and K+ release to the cytoplasm.
"This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm"
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Asp307 substitutions abolish phosphoenzyme formation and ATPase activity.
"D->E,N,Q: Unable to form a phosphorylated intermediate and lacks ATPase activity."
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Ser162 phosphorylation inhibits ATPase activity.
"ATPase activity is inhibited by phosphorylation at Ser-162"
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KdpB belongs to the type IA P-type ATPase family.
"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily."
UniProtKB P03960 (KDPB_ECOLI) record
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KdpB is responsible for energy coupling and K+ release to the cytoplasm.
"This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm"
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Asp307 substitutions abolish phosphoenzyme formation and ATPase activity.
"D->E,N,Q: Unable to form a phosphorylated intermediate and lacks ATPase activity."
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Ser162 phosphorylation inhibits ATPase activity.
"ATPase activity is inhibited by phosphorylation at Ser-162"
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KdpB belongs to the type IA P-type ATPase family.
"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily."
UniProtKB P03960 (KDPB_ECOLI) record
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KdpB is responsible for energy coupling and K+ release to the cytoplasm.
"This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm"
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Asp307 substitutions abolish phosphoenzyme formation and ATPase activity.
"D->E,N,Q: Unable to form a phosphorylated intermediate and lacks ATPase activity."
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Ser162 phosphorylation inhibits ATPase activity.
"ATPase activity is inhibited by phosphorylation at Ser-162"
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KdpB belongs to the type IA P-type ATPase family.
"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily."