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16000
-
SDS-PAGE, KdpCsol cleavage product
20000
-
1 * 59000 + 1 * 72000 + 1 * 20000 + 1 * 3000, SDS-PAGE
20267
-
1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis
21000
-
1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
23500
-
1 * 70000 + 1 * 43500 + 1 * 23500, SDS-PAGE
43500
-
1 * 70000 + 1 * 43500 + 1 * 23500, SDS-PAGE
47000
-
1 * 47000 + 1 * 90000 + 1 * 22000, SDS-PAGE
58189
-
1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis
70000
-
1 * 70000 + 1 * 43500 + 1 * 23500, SDS-PAGE
72112
-
1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis
90000
-
1 * 47000 + 1 * 90000 + 1 * 22000, SDS-PAGE
122200
calculated from sequence of cDNA
128400
calculated from sequence of cDNA
129500
Udotea petiolata
-
calculated from sequence of cDNA
150600
-
DNA-sequence analysis
350000
-
gel filtration, KdpFABC complex, a cross-linked preparation
22000

-
1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
22000
-
1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
22000
-
1 * 47000 + 1 * 90000 + 1 * 22000, SDS-PAGE
59000

-
1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
59000
-
1 * 59000 + 1 * 72000 + 1 * 20000 + 1 * 3000, SDS-PAGE
72000

-
1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
72000
-
1 * 59000 + 1 * 72000 + 1 * 20000 + 1 * 3000, SDS-PAGE
72000
-
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
74000

-
1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
74000
-
1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
79000

-
1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
79000
-
1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
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DELTAkdpX
-
truncation of the kdpX gene leads to a less efficient K+-pump than wild-type
DELTAkdpY
-
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
-
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
-
loss of K+ transport
A220F
-
lower affinity to K+ than wild-type
A220K
-
lower affinity to K+ than wild-type
A220P
-
lower affinity to K+ than wild-type
A220S
-
lower affinity to K+ than wild-type
A220Y
-
lower affinity to K+ than wild-type
A224H
-
lower affinity to K+ than wild-type
A224K
-
lower affinity to K+ than wild-type
A224Q
-
lower affinity to K+ than wild-type
A341K
-
lower affinity to K+ than wild-type
A342K
-
lower affinity to K+ than wild-type
A346K
-
lower affinity to K+ than wild-type
A346Y
-
lower affinity to K+ than wild-type
A459K
-
lower affinity to K+ than wild-type
A464H
-
lower affinity to K+ than wild-type
A464K
-
lower affinity to K+ than wild-type
A464L
-
lower affinity to K+ than wild-type
A464P
-
lower affinity to K+ than wild-type
A464Y
-
lower affinity to K+ than wild-type
C344K
-
lower affinity to K+ than wild-type
C344P
-
lower affinity to K+ than wild-type
D352K
-
lower affinity to K+ than wild-type
E223K
-
lower affinity to K+ than wild-type
E223P
-
lower affinity to K+ than wild-type
F235K
-
lower affinity to K+ than wild-type
F236K
-
lower affinity to K+ than wild-type
F335K
-
lower affinity to K+ than wild-type
F354G
-
lower affinity to K+ than wild-type
F471E
-
lower affinity to K+ than wild-type
F471K
-
lower affinity to K+ than wild-type
F471P
-
lower affinity to K+ than wild-type
F471Y
-
lower affinity to K+ than wild-type
G120K
-
lower affinity to K+ than wild-type
G217A
-
lower affinity to K+ than wild-type
G217K
-
lower affinity to K+ than wild-type
G229H
-
lower affinity to K+ than wild-type
G229K
-
lower affinity to K+ than wild-type
G232A
-
lower affinity to K+ than wild-type
G232C
-
lower affinity to K+ than wild-type
G232E
-
lower affinity to K+ than wild-type
G232H
-
lower affinity to K+ than wild-type
G232K
-
lower affinity to K+ than wild-type
G232L
-
lower affinity to K+ than wild-type
G232P
-
lower affinity to K+ than wild-type
G232Q
-
lower affinity to K+ than wild-type
G232S
-
lower affinity to K+ than wild-type
G232Y
-
lower affinity to K+ than wild-type
G233E
-
lower affinity to K+ than wild-type
G233K
-
lower affinity to K+ than wild-type
G233P
-
lower affinity to K+ than wild-type
G233Q
-
lower affinity to K+ than wild-type
G233Y
-
lower affinity to K+ than wild-type
G234K
-
lower affinity to K+ than wild-type
G234P
-
lower affinity to K+ than wild-type
G358K
-
lower affinity to K+ than wild-type
G468K
-
lower affinity to K+ than wild-type
I225K
-
lower affinity to K+ than wild-type
I348C
-
lower affinity to K+ than wild-type
I348F
-
lower affinity to K+ than wild-type
I348K
-
lower affinity to K+ than wild-type
I348P
-
lower affinity to K+ than wild-type
I348Y
-
lower affinity to K+ than wild-type
I367K
-
lower affinity to K+ than wild-type
K226P
-
lower affinity to K+ than wild-type
L228K
-
lower affinity to K+ than wild-type
L330K
-
lower affinity to K+ than wild-type
L365K
-
lower affinity to K+ than wild-type
M366K
-
lower affinity to K+ than wild-type
N112K
-
lower affinity to K+ than wild-type
N112P
-
lower affinity to K+ than wild-type
N114E
-
lower affinity to K+ than wild-type
N114F
-
lower affinity to K+ than wild-type
N114H
-
lower affinity to K+ than wild-type
N114K
-
lower affinity to K+ than wild-type
N114L
-
lower affinity to K+ than wild-type
N114P
-
lower affinity to K+ than wild-type
N114Q
-
lower affinity to K+ than wild-type
N114S
-
lower affinity to K+ than wild-type
N114Y
-
lower affinity to K+ than wild-type
N231K
-
lower affinity to K+ than wild-type
N231P
-
lower affinity to K+ than wild-type
N231Y
-
lower affinity to K+ than wild-type
N237K
-
lower affinity to K+ than wild-type
N239H
-
lower affinity to K+ than wild-type
N239K
-
lower affinity to K+ than wild-type
N465K
-
lower affinity to K+ than wild-type
N466K
-
lower affinity to K+ than wild-type
N467K
-
lower affinity to K+ than wild-type
P362K
-
lower affinity to K+ than wild-type
Q116H
-
lower affinity to K+ than wild-type
Q116K
-
lower affinity to K+ than wild-type
Q116P
-
lower affinity to K+ than wild-type
Q116R
-
mutant with reduced affinity for K+
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
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
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
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
Q222K
-
lower affinity to K+ than wild-type
S119K
-
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
-
mutant with reduced affinity for K+
-
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
additional information
-
expression of plasmid-encoded kdpFABCcat3 is sufficient to complement the phenotype of a chromosomal kdpFABCcat3 deletion strain, whereas expression of only kdpFABC is not
additional information
-
expression of plasmid-encoded kdpFABCcat3 is sufficient to complement the phenotype of a chromosomal kdpFABCcat3 deletion strain, whereas expression of only kdpFABC is not
-
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Harvey, W.R.; Cioffi, M.; Dow, J.A.T.; Wolfersberger, M.G.
Potassium ion transport ATPase in insect epithelia
J. Exp. Biol.
106
91-117
1983
Jamaicana flava, Locusta migratoria, Manduca sexta, Schistocerca gregaria
brenda
Siebers, A.; Altendorf, K.
The K+-translocating Kdp-ATPase from Escherichia coli. Purification, enzymatic properties and production of complex- and subunit-specific antisera
Eur. J. Biochem.
178
131-140
1988
Escherichia coli, Escherichia coli TKA 1000
brenda
Hafer, J.; Siebers, A.; Bakker, E.P.
The high-affinity K+-translocating ATPase complex from Bacillus acidocaldarius consists of three subunits
Mol. Microbiol.
3
487-495
1989
Alicyclobacillus acidocaldarius
brenda
Siebers, A.; Altendorf, K.
Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli
J. Biol. Chem.
264
5831-5838
1989
Escherichia coli, Escherichia coli TKA 1000
brenda
Siebers, A.; Kollmann, R.; Dierkes, G.; Altendorf, K.
Rapid, high yield purification and characterization of the K+-translocating Kdp-ATPase from Escherichia coli
J. Biol. Chem.
257
12717-12721
1992
Escherichia coli, Escherichia coli TKA 1000
-
brenda
Abee, T.; Siebers, A.; Altendorf, K.; Konings, W.N.
Isolation and characterization of the high-affinity K+-translocating ATPase from Rhodobacter sphaeroides
J. Bacteriol.
174
6911-6917
1992
Rhodobacter sphaeroides
brenda
Epstein, W.; Wieczorek, L.; Siebers, A.; Altendorf, K.
Potassium transport in Escherichia coli: genetic and biochemical characterization of the K+-transporting ATPase
Biochem. Soc. Trans.
12
235-236
1984
Escherichia coli
brenda
Kollmann, R.; Altendorf, K.
ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli
Biochim. Biophys. Acta
1143
62-66
1993
Escherichia coli, Escherichia coli TKA 1000
brenda
Fendler, K.; Dröse, S.; Altendorf, K.; Bamberg, E.
Electrogenic K+ transport by the Kdp-ATPase of Escherichia coli
Biochemistry
35
8009-8017
1996
Escherichia coli, Escherichia coli TKA 1000
brenda
Iwane, A.H.; Ikeda, I.; Kimura, Y.; Fujiyoshi, Y.; Altendorf, K.; Epstein, W.
Two-dimensional crystals of the Kdp-ATPase of Escherichia coli
FEBS Lett.
396
172-176
1996
Escherichia coli, Escherichia coli TK 2242/pSR5
brenda
Ga¯el, M.; Möllenkamp, T.; Puppe, W.; Altendorf, K.
The KdpF subunit is part of the K+-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro
J. Biol. Chem.
274
37901-37907
1999
Escherichia coli, Escherichia coli TKW3205/pSR5
brenda
Fendler, K.; Dröse, S.; Epstein, W.; Bamberg, E.; Altendorf, K.
The Kdp-ATPase of Escherichia coli mediates an ATP-dependent, K+-independent electrogenic partial reaction
Biochemistry
38
1850-1856
1999
Escherichia coli, Escherichia coli TKA 1000
brenda
Durell, S.R.; Bakker, E.P.; Guy, H.R.
Does the KdpA subunit from the high affinity K+-translocating P-type KDP-ATPase have a structure similar to that of K+ channels?
Biophys. J.
78
188-199
2000
Alicyclobacillus acidocaldarius (Q9XE11), Clostridium acetobutylicum (O32327), Escherichia coli (P03959), Mycobacterium tuberculosis, Synechocystis sp. PCC 6803 (P73866)
brenda
Behrens, M.; Schreiber, W.; Durre, P.
The high-affinity K-translocating ATPase complex from Clostridium acetobutylicum consists of six subunits
Anaerobe
7
159-169
2001
Clostridium acetobutylicum
-
brenda
Sebestian, J.; Petrmichlova, Z.; Sebestianova, S.; Naprstek, J.; Svobodova, J.
Osmoregulation in Bacillus subtilis under potassium limitation: a new inducible K+-stimulated, VO4(3-)-inhibited ATPase
Can. J. Microbiol.
47
1116-1125
2001
Bacillus subtilis
brenda
Gassel, M.; Altendorf, K.
Analysis of KdpC of the K+ -transporting KdpFABC complex of Escherichia coli
Eur. J. Biochem.
268
1772-1781
2001
Escherichia coli
brenda
Sardesai, A.A.; Gowrishankar, J.
Improvement in K+-limited growth rate associated with expression of the N-terminal fragment of one subunit (KdpA) of the multisubunit Kdp transporter in Escherichia coli
J. Bacteriol.
183
3515-3520
2001
Escherichia coli
brenda
Dorus, S.; Mimura, H.; Epstein, W.
Substrate-binding clusters of the K+-transporting Kdp ATPase of Escherichia coli investigated by amber suppression scanning mutagenesis
J. Biol. Chem.
276
9590-9598
2001
Escherichia coli
brenda
Ahnert, F.; Schmid, R.; Altendorf, K.; Greie, J.C.
ATP binding properties of the soluble part of the KdpC subunit from the Escherichia coli K(+)-transporting KdpFABC P-type ATPase
Biochemistry
45
11038-11046
2006
Escherichia coli
brenda
De Hertogh, B.; Lantin, A.; Baret, P.V.; Goffeau, A.
The Archaeal P-Type ATPases
J. Bioenerg. Biomembr.
36
135-142
2004
Ferroplasma acidarmanus, Halobacterium sp., Thermoplasma acidophilum (P57700), Thermoplasma volcanium (Q97BF6)
brenda
Barrero-Gil, J.; Garciadeblas, B.; Benito, B.
Sodium, potassium-atpases in algae and oomycetes
J. Bioenerg. Biomembr.
37
269-278
2005
Pyropia yezoensis (Q4LB57), Pythium aphanidermatum (Q4LB39), Pythium aphanidermatum 356128 (Q4LB39), Udotea petiolata
brenda
Heitkamp, T.; Kalinowski, R.; Boettcher, B.; Boersch, M.; Altendorf, K.; Greie, J.
K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer
Biochemistry
47
3564-3575
2008
Escherichia coli
brenda
Vagabov, V.M.; Ivanov, A.Y.; Kulakovskaya, T.V.; Kulakovskaya, E.V.; Petrov, V.V.; Kulaev, I.S.
Efflux of potassium ions from cells and spheroplasts of Saccharomyces cerevisiae yeast treated with silver and copper ions
Biochemistry (Moscow)
73
1224-1227
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
brenda
Strahl, H.; Greie, J.C.
The extremely halophilic archaeon Halobacterium salinarum R1 responds to potassium limitation by expression of the K+-transporting KdpFABC P-type ATPase and by a decrease in intracellular K+
Extremophiles
12
741-752
2008
Halobacterium salinarum, Halobacterium salinarum R1
brenda
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
FEBS J.
278
3041-3053
2011
Escherichia coli
brenda