Information on EC 3.6.3.12 - K+-transporting ATPase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
3.6.3.12
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RECOMMENDED NAME
GeneOntology No.
K+-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + K+/out = ADP + phosphate + K+/in
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (K+-importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme of di(heterotetrameric) structure that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain TK 2242/pSR5
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-
Manually annotated by BRENDA team
strain TKW3205/pSR5
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-
Manually annotated by BRENDA team
strain R1
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-
Manually annotated by BRENDA team
strain R1
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Jamaicana flava
Orthoptera
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
red alga
SwissProt
Manually annotated by BRENDA team
strain 356128oomycete
SwissProt
Manually annotated by BRENDA team
strain 356128oomycete
SwissProt
Manually annotated by BRENDA team
strain VKM Y-1173
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-
Manually annotated by BRENDA team
strain VKM Y-1173
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Manually annotated by BRENDA team
Udotea petiolata
green alga
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the ATP-hydrolyzing subunit KdpB in the transport complex is classified as type IA P-type ATPase
physiological function
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high-affinity potassium uptake is mediated by the ATP-driven KdpFABC complex. The KdpA subunit promotes K+ transport
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + K+/out
ADP + phosphate + K+/in
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + K+/out
ADP + phosphate + K+/in
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
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induces the efflux of potassium ions from cells
Cu2+
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induces the efflux of potassium ions from both cells and spheroplasts
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bafilomycin A1
concanamycin A
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Fluorescein isothiocyanate
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N,N'-dicyclohexylcarbodiimide
N-ethylmaleimide
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ortho-vanadate
small peptides from Bacillus thuringiensis
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vanadate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-O-3-hydroxyhexanoyl-beta-D-glucopyranosyl(1-4)-(6-O-acetyl-beta-D-glucopyranosyl(1-16)-2,15,16-trihydroxyhexadecanoic acid)
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a natural fungicide, i.e. CL, produced by the yeast Pseudozyma fusiformata VKM Y-2821, induces the efflux of potassium ions from both cells and spheroplasts
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Cat3 protein
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required for enzyme gene cluster expression and activity, encoded by an additional ORF located immediately downstream of the kdpFABC gene cluster, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
ATP
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37°C, pH 7.8
0.002 - 0.025
K+
0.08
MgATP2-
additional information
additional information
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kinetics
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
vanadate
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37°C, pH 7.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0339
Jamaicana flava
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0.56
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addition of K+
597
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wild-type with His-tag
additional information
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ATPase activity and ATP binding affinity of wild-type and mutant enzyme complexes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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SDS-PAGE, KdpCsol cleavage product
20000
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1 * 59000 + 1 * 72000 + 1 * 20000 + 1 * 3000, SDS-PAGE
20267
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1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis
21000
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1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
23500
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1 * 70000 + 1 * 43500 + 1 * 23500, SDS-PAGE
43500
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1 * 70000 + 1 * 43500 + 1 * 23500, SDS-PAGE
47000
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1 * 47000 + 1 * 90000 + 1 * 22000, SDS-PAGE
58189
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1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis
70000
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1 * 70000 + 1 * 43500 + 1 * 23500, SDS-PAGE
72112
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1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis
90000
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1 * 47000 + 1 * 90000 + 1 * 22000, SDS-PAGE
122200
calculated from sequence of cDNA
128400
calculated from sequence of cDNA
129500
Udotea petiolata
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calculated from sequence of cDNA
137000
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SDS-PAGE
150600
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DNA-sequence analysis
154000
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gel filtration
175000
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SDS-PAGE
350000
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gel filtration, KdpFABC complex, a cross-linked preparation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 72000, SDS-PAGE, functional and structural dimeric enzyme with a close vicinity of two KdpB subunits within the functional KdpFABC complex, a dissociation constant for a monomer/dimer equilibrium between 30 and 50 nM, structure, overview
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration and affinity resin column chromatography
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recombinant wild-type and mutant enzyme complexes from Escherichia coli strain BL21
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and expression of wild-type and mutant enzyme complexes in Escherichia coli strain BL21
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expressed in Escherichia coli
expressed in Saccharomyces cerevisiae
expression in Escherichia coli
expression of wild-type and mutant enzymes in strain TKW3205
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kdpFABC gene cluster, strain R1 comprises one single gene cluster containing the genes kdpFABC coding for homologs of the bacterial ATP-driven K+ uptake system KdpFABC, genes kdpB and kdpC as well as kdpC and cat3 do overlap by one base pair, genetic organization and regulation, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAkdpX
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truncation of the kdpX gene leads to a less efficient K+-pump than wild-type
DELTAkdpY
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truncation of the kdpY gene has a significant impact on the growth of the Escherichia coli mutant TK2205, which is unable to grow at low potassium concentrations
DELTAkdpZ
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truncation of the kdpZ gene has a significant impact on the growth of the Escherichia coli mutant TK2205, which is unable to grow at low potassium concentrations
DELTAkdpZY
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loss of K+ transport
A220F
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lower affinity to K+ than wild-type
A220K
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lower affinity to K+ than wild-type
A220P
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lower affinity to K+ than wild-type
A220S
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lower affinity to K+ than wild-type
A220Y
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lower affinity to K+ than wild-type
A224H
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lower affinity to K+ than wild-type
A224K
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lower affinity to K+ than wild-type
A224Q
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lower affinity to K+ than wild-type
A341K
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lower affinity to K+ than wild-type
A342K
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lower affinity to K+ than wild-type
A346K
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lower affinity to K+ than wild-type
A346Y
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lower affinity to K+ than wild-type
A459K
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lower affinity to K+ than wild-type
A464H
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lower affinity to K+ than wild-type
A464K
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lower affinity to K+ than wild-type
A464L
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lower affinity to K+ than wild-type
A464P
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lower affinity to K+ than wild-type
A464Y
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lower affinity to K+ than wild-type
C344K
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lower affinity to K+ than wild-type
C344P
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lower affinity to K+ than wild-type
D352K
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lower affinity to K+ than wild-type
E223K
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lower affinity to K+ than wild-type
E223P
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lower affinity to K+ than wild-type
F235K
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lower affinity to K+ than wild-type
F236K
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lower affinity to K+ than wild-type
F335K
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lower affinity to K+ than wild-type
F354G
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lower affinity to K+ than wild-type
F471E
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lower affinity to K+ than wild-type
F471K
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lower affinity to K+ than wild-type
F471P
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lower affinity to K+ than wild-type
F471Y
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lower affinity to K+ than wild-type
G120K
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lower affinity to K+ than wild-type
G217A
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lower affinity to K+ than wild-type
G217K
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lower affinity to K+ than wild-type
G229H
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lower affinity to K+ than wild-type
G229K
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lower affinity to K+ than wild-type
G232A
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lower affinity to K+ than wild-type
G232C
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lower affinity to K+ than wild-type
G232E
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lower affinity to K+ than wild-type
G232H
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lower affinity to K+ than wild-type
G232K
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lower affinity to K+ than wild-type
G232L
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lower affinity to K+ than wild-type
G232P
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lower affinity to K+ than wild-type
G232Q
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lower affinity to K+ than wild-type
G232S
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lower affinity to K+ than wild-type
G232Y
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lower affinity to K+ than wild-type
G233E
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lower affinity to K+ than wild-type
G233K
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lower affinity to K+ than wild-type
G233P
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lower affinity to K+ than wild-type
G233Q
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lower affinity to K+ than wild-type
G233Y
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lower affinity to K+ than wild-type
G234K
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lower affinity to K+ than wild-type
G234P
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lower affinity to K+ than wild-type
G358K
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lower affinity to K+ than wild-type
G468K
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lower affinity to K+ than wild-type
I225K
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lower affinity to K+ than wild-type
I348C
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lower affinity to K+ than wild-type
I348F
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lower affinity to K+ than wild-type
I348K
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lower affinity to K+ than wild-type
I348P
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lower affinity to K+ than wild-type
I348Y
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lower affinity to K+ than wild-type
I367K
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lower affinity to K+ than wild-type
K226P
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lower affinity to K+ than wild-type
L228K
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lower affinity to K+ than wild-type
L330K
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lower affinity to K+ than wild-type
L365K
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lower affinity to K+ than wild-type
M366K
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lower affinity to K+ than wild-type
N112K
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lower affinity to K+ than wild-type
N112P
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lower affinity to K+ than wild-type
N114E
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lower affinity to K+ than wild-type
N114F
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lower affinity to K+ than wild-type
N114H
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lower affinity to K+ than wild-type
N114K
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lower affinity to K+ than wild-type
N114L
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lower affinity to K+ than wild-type
N114P
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lower affinity to K+ than wild-type
N114Q
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lower affinity to K+ than wild-type
N114S
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lower affinity to K+ than wild-type
N114Y
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lower affinity to K+ than wild-type
N231K
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lower affinity to K+ than wild-type
N231P
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lower affinity to K+ than wild-type
N231Y
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lower affinity to K+ than wild-type
N237K
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lower affinity to K+ than wild-type
N239H
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lower affinity to K+ than wild-type
N239K
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lower affinity to K+ than wild-type
N465K
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lower affinity to K+ than wild-type
N466K
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lower affinity to K+ than wild-type
N467K
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lower affinity to K+ than wild-type
P362K
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lower affinity to K+ than wild-type
Q116H
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lower affinity to K+ than wild-type
Q116K
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lower affinity to K+ than wild-type
Q116P
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lower affinity to K+ than wild-type
Q116R
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mutant with reduced affinity for K+
Q140A
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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
Q140A/R143A/V144A/A145S/A147S/R148A/L150A
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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
Q140E
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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
Q140N
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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
Q222K
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lower affinity to K+ than wild-type
S119K
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lower affinity to K+ than wild-type
S221K
-
lower affinity to K+ than wild-type
S343F
-
lower affinity to K+ than wild-type
S343K
-
lower affinity to K+ than wild-type
S343L
-
lower affinity to K+ than wild-type
S343Y
-
lower affinity to K+ than wild-type
S461F
-
lower affinity to K+ than wild-type
S461K
-
lower affinity to K+ than wild-type
S461Y
-
lower affinity to K+ than wild-type
S469G
-
lower affinity to K+ than wild-type
S469H
-
lower affinity to K+ than wild-type
S469K
-
lower affinity to K+ than wild-type
S469L
-
lower affinity to K+ than wild-type
S469P
-
lower affinity to K+ than wild-type
S469Q
-
lower affinity to K+ than wild-type
S469Y
-
lower affinity to K+ than wild-type
T111G
-
lower affinity to K+ than wild-type
T111K
-
lower affinity to K+ than wild-type
T113F
-
lower affinity to K+ than wild-type
T113K
-
lower affinity to K+ than wild-type
T113P
-
lower affinity to K+ than wild-type
T113Y
-
lower affinity to K+ than wild-type
T230K
-
lower affinity to K+ than wild-type
T230Y
-
lower affinity to K+ than wild-type
T339H
-
lower affinity to K+ than wild-type
T339K
-
lower affinity to K+ than wild-type
T339Q
-
lower affinity to K+ than wild-type
T340F
-
lower affinity to K+ than wild-type
T340K
-
lower affinity to K+ than wild-type
T340Y
-
lower affinity to K+ than wild-type
T355A
-
lower affinity to K+ than wild-type
T355K
-
lower affinity to K+ than wild-type
V110K
-
lower affinity to K+ than wild-type
V331K
-
lower affinity to K+ than wild-type
V337K
-
lower affinity to K+ than wild-type
W115K
-
lower affinity to K+ than wild-type
Y458K
-
lower affinity to K+ than wild-type
Q116R
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mutant with reduced affinity for K+
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additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of functional dimeric KdpFABC complexes, overview
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