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Literature summary for 7.2.2.6 extracted from

  • Irzik, K.; Pfroetzschner, J.; Goss, T.; Ahnert, F.; Haupt, M.; Greie, J.C.
    The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone (2011), FEBS J., 278, 3041-3053.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloning and expression of wild-type and mutant enzyme complexes in Escherichia coli strain BL21 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the 140-QIPRVAKARNL-150 ATP binding motif in KdpC is deleted completely, resulting in mutant DELTAQ-L, cells comprising a deletion of the signature motif showed no growth if the potassium concentration drops below 5 mM. The mutations generated result in different phenotypes with respect to tolerance of potassium limitation, overview Escherichia coli
Q140A site-directed mutagenesis, the mutant is still able to tolerate extreme potassium limitations below 0.1 mM, but shows 38% reduced growth compared to the wild-type Escherichia coli
Q140A/R143A/V144A/A145S/A147S/R148A/L150A site-directed mutagenesis of the complete 140-QIPRVAKARNL-150 ATP binding motif in KdpC, the mutant cells comprising a complete exchange of the signature motif show no growth if the potassium concentration drops below 5 mM Escherichia coli
Q140E site-directed mutagenesis, the mutant is still able to tolerate extreme potassium limitations below 0.1 mM, but shows 38% reduced growth compared to the wild-type Escherichia coli
Q140N site-directed mutagenesis, the mutant is still able to tolerate extreme potassium limitations below 0.1 mM, but shows 12% reduced growth compared to the wild-type Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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strain TKW3205
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Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzyme complexes from Escherichia coli strain BL21 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
ATPase activity and ATP binding affinity of wild-type and mutant enzyme complexes, overview Escherichia coli

Synonyms

Synonyms Comment Organism
K+-transporting KdpB P-type ATPase
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Escherichia coli

General Information

General Information Comment Organism
evolution the ATP-hydrolyzing subunit KdpB in the transport complex is classified as type IA P-type ATPase Escherichia coli
physiological function high-affinity potassium uptake is mediated by the ATP-driven KdpFABC complex. The KdpA subunit promotes K+ transport Escherichia coli