Literature summary 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.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
7.2.2.6 |
cloning and expression of wild-type and mutant enzyme complexes in Escherichia coli strain BL21 |
Escherichia coli |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
7.2.2.6 |
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 |
7.2.2.6 |
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 |
7.2.2.6 |
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 |
7.2.2.6 |
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 |
7.2.2.6 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
7.2.2.6 |
Escherichia coli |
- |
strain TKW3205 |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
7.2.2.6 |
recombinant wild-type and mutant enzyme complexes from Escherichia coli strain BL21 |
Escherichia coli |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
7.2.2.6 |
additional information |
- |
ATPase activity and ATP binding affinity of wild-type and mutant enzyme complexes, overview |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
7.2.2.6 |
K+-transporting KdpB P-type ATPase |
- |
Escherichia coli |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
7.2.2.6 |
evolution |
the ATP-hydrolyzing subunit KdpB in the transport complex is classified as type IA P-type ATPase |
Escherichia coli |
7.2.2.6 |
physiological function |
high-affinity potassium uptake is mediated by the ATP-driven KdpFABC complex. The KdpA subunit promotes K+ transport |
Escherichia coli |