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Information on EC 7.2.2.1 - Na+-transporting two-sector ATPase
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7.2.2.1 Na+-transporting two-sector ATPaseIUBMB Comments
A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis. The enzyme is similar to EC 7.1.2.2 (H+-transporting two-sector ATPase) but pumps Na+ rather than H+. By analogy to EC 7.1.2.2, it is likely that the enzyme pumps 4 sodium ions for every ATP molecule that is hydrolysed. cf. EC 7.2.2.3, P-type Na+ transporter and EC 7.2.2.4, ABC-type Na+ transporter.
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Word Map
- 7.2.2.1
- ouabain
-
electrogenic
-
k+-atpase
-
depolarization
-
ouabain-sensitive
-
basolateral
-
hyperpolarization
- na+,k+-atpase
-
transepithelial
- amiloride
-
na+-dependent
-
k+-free
-
microelectrodes
-
na+-pumping
- hirae
- rb+
-
sarcolemmal
-
na+-stimulated
-
short-circuit
- alginolyticus
-
na+-k+-adenosinetriphosphatase
-
3h-ouabain
-
low-na+
-
digitalis-like
-
ouabain-inhibitable
-
ouabain-induced
- dccd
-
na+-sensitive
-
nadh:quinone
- strophanthidin
- isophthalate
-
na+-loaded
-
countertransport
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
na+ pump, na+-atpase, f-type atp synthase, umpab, na+-translocating atpase, v-type na+-atpase, na+-translocating v-atpase, vacuole-type atpase, vacuolar-type na+-translocating atpase, na+-transporting p-type atpase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A1AO ATP synthase
ATP phosphohydrolase (Na+-transporting)
-
-
ambiguous
-
ATP synthase
-
-
-
-
EC 3.6.3.15
-
-
formerly
-
F1FO-ATPase
Lipid-binding protein
-
-
-
-
Na+ pump
Na+ V-ATPase
-
Na+(Li+, K+)/H+ antiporter
Na+-ATPase
Na+-translocating ATPase
Na+-translocating F1FO-ATPase
Na+-transporting P-type ATPase
Na+-transporting two-sector ATPase
-
-
ambiguous
-
Ntp
-
UmpAB
vacuolar-type Na+-ATPase
-
-
-
-
vacuolar-type Na+-translocating ATPase
-
-
-
-
Na+-translocating ATPase
-
-
-
-
Na+-translocating F1FO-ATPase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (two-sector, Na+-transporting)
A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis. The enzyme is similar to EC 7.1.2.2 (H+-transporting two-sector ATPase) but pumps Na+ rather than H+. By analogy to EC 7.1.2.2, it is likely that the enzyme pumps 4 sodium ions for every ATP molecule that is hydrolysed. cf. EC 7.2.2.3, P-type Na+ transporter and EC 7.2.2.4, ABC-type Na+ transporter.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Li+/in
ADP + phosphate + Li+/out
-
coupled to Li+ translocation across the cytoplasmic membrane
-
-
?
CDP + phosphate + Na+/out
CTP + H2O + Na+/in
-
lower activity compared to ADP
-
-
r
CTP + H2O + Na+/in
CDP + phosphate + Na+/out
-
CTP is hydrolyzed at 14% compared to hydrolysis of ATP
-
-
?
GDP + phosphate + Na+/out
GTP + H2O + Na+/in
-
lower activity compared to ADP
-
-
r
GTP + H2O + Na+/in
GDP + phosphate + Na+/out
-
GTP is hydrolyzed at 64% compared to hydrolysis of ATP
-
-
?
IDP + phosphate + Na+/out
ITP + H2O + Na+/in
-
lower activity compared to ADP
-
-
r
ITP + H2O + Na+/in
IDP + phosphate + Na+/out
-
ITP is hydrolyzed at 99% compared to hydrolysis of ATP
-
-
?
UDP + phosphate + Na+/out
UTP + H2O + Na+/in
-
lower activity compared to ADP
-
-
r
UTP + H2O + Na+/in
UDP + phosphate + Na+/out
-
UTP is hydrolyzed at 31% compared to hydrolysis of ATP
-
-
?
ADP + phosphate
ATP
-
Na+-translocating ATPase can work in the synthase mode under alkaline conditions
-
-
r
ADP + phosphate
ATP
-
Na+-translocating ATPase can work in the synthase mode under alkaline conditions
-
-
r
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
the V-type ATPase pumps Na+ ions out of the cell against the sodium ion motive force at the expense of the hydrolysis of ATP. The enzyme complex consists of an integral membrane part V0 that is responsible for the translocation of the Na+ ions and a cytoplasmic, membrane associated part V1 that hydrolyzes ATP, it functions as two coupled molecular motors
-
-
ir
ATP + H2O
ADP + phosphate
-
nucleotides are hydrolyzed in the order of decreasing activity: GTP, CTP, UTP, ATP
-
-
?
ATP + H2O
ADP + phosphate
-
Na+-translocating ATPase can work in the synthase mode under alkaline conditions
-
-
r
ATP + H2O
ADP + phosphate
-
Na+-translocating ATPase can work in the synthase mode under alkaline conditions
-
-
r
ATP + H2O + n K+[side 1]
ADP + phosphate + n K+[side 2]
Halomonas zhaodongensis NEAU-ST10-25T
-
-
-
-
?
ATP + H2O + n Li+[side 1]
ADP + phosphate + n Li+[side 2]
Halomonas zhaodongensis NEAU-ST10-25T
-
-
-
-
?
ATP + H2O + n Na+[side 1]
ADP + phosphate + n Na+[side 2]
Halomonas zhaodongensis NEAU-ST10-25T
-
-
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
coupled to Na+ translocation across the cytoplasmic membrane
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
the purified rotor ring, i.e. K-ring, of the V-ATPase binds one Na+ ion per K-monomer with high affinity. Interaction with the stator subunit, i.e. I-subunit, is essential for Na binding to or release from the K-ring, respectively, ion translocation model, overview
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
ATP hydrolysis is strictly dependent on Na+, with a Km of 0.6 mM. Li+, but not K+, can substitute for Na+. The Na+ dependence is less pronounced at higher proton concentrations, indicating competition between Na+ and H+ for a common binding site
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
-
the enzyme reconstituted in proteoliposomes, generated from Escherichia coli lipids, catalyzes ATP-driven Na+ transport
-
-
?
CTP + H2O
CDP + H2O
-
nucleotides are hydrolyzed in the order of decreasing activity: GTP, CTP, UTP, ATP
-
-
?
GTP + H2O
GDP + phosphate
-
hydrolyzed at 31% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
-
Na+-translocating activity, GTP is hydrolyzed as the best substrate
-
-
?
UTP + H2O
UDP + H2O
-
nucleotides are hydrolyzed in the order of decreasing activity: GTP, CTP, UTP, ATP
-
-
?
additional information
?
-
-
the length of the C-terminus as well as specific residues located in the cytoplasmic membrane are important for Na+ transport
-
-
?
additional information
?
-
-
Glu139 of the NtpK proteolipid subunit is binding site of Na+ or Li+ for translocation
-
-
?
additional information
?
-
-
the transcription of the Na+-ATPase operon is regulated by the intracellular concentration of Na+
-
-
?
additional information
?
-
-
enzyme is induced when cells are grown on media rich in sodium
-
-
?
additional information
?
-
-
K+, Tl+, Rb+, and Cs+ cannot substitute Na+
-
-
?
additional information
?
-
-
Na+-translocation involves a minimum of four steps: 1. binding of Na+ from a defined surface of the membrane, translocation of the binary complex to the outer surface, 3. release of Na+, 4. return of the unloaded carrier to the original surface
-
-
?
additional information
?
-
-
neither ADP nor diphosphate are hydrolyzed
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
the V-type ATPase pumps Na+ ions out of the cell against the sodium ion motive force at the expense of the hydrolysis of ATP. The enzyme complex consists of an integral membrane part V0 that is responsible for the translocation of the Na+ ions and a cytoplasmic, membrane associated part V1 that hydrolyzes ATP, it functions as two coupled molecular motors
-
-
ir
ATP + H2O + n Na+[side 1]
ADP + phosphate + n Na+[side 2]
Halomonas zhaodongensis NEAU-ST10-25T
-
-
-
-
?
additional information
?
-
-
the transcription of the Na+-ATPase operon is regulated by the intracellular concentration of Na+
-
-
?
additional information
?
-
-
enzyme is induced when cells are grown on media rich in sodium
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Cu2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Li+
Mg2+
Mn2+
Na+
Ni2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
NO3-
Zn2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Li+
-
75% of the maximal activity compared to saturating Na+ concentrations
Li+
-
enzyme activity is strictly dependent on the presence of Na+ or Li+ ions
Mg2+
-
activity is dependent on MgATP, at pH 8.5 optimal Mg2+ concentration is 2 mM
Mg2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Mg2+
-
the enzyme requires divalent cations for activity, highest stimulation is with Mn2+ followed by Mg2+ and Co2+ (10 mM each)
Mn2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Mn2+
-
the enzyme requires divalent cations for activity, highest stimulation is with Mn2+ followed by Mg2+ and Co2+ (10 mM each)
Na+
-
the enzyme has Na+-translocating activity
Na+
-
enzyme activity is strictly dependent on the presence of Na+ or Li+ ions
Na+
-
6 Na+ are bound per enzyme molecule by a singly high affinity, about two-thirds of the Na+ binding sites of the Na+ ATPase are readily acessible from the aqueous phase
Na+
-
the enzyme has Na+-translocating activity
Na+
-
three to fourfold stimulation of activity at pH 7.0, five to sixfold stimulation of activity at pH 9.0
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(N,N-Hexamethylene)amiloride
-
70% inhibition at 0.1 mM, Na+ protects against inactivation
5-(N-ethyl-N-isopropyl)amiloride
-
70% inhibition at 0.1 mM, Na+ protects against inactivation
ATPgammaS
-
inhibits ATPase activity but not the Na+ binding capacity of the enzyme
Carbonyl cyanide m-chlorophenylhydrazone
-
0.02 mM, pH 9.0, 75% inhibition with no or low levels of NaCl
H+
-
competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview
Li+
-
competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview
N,N'-dicyclohexyl-carbodiimide
-
half maximal inhibition at 0.1 mM. N,N'-dicyclohexyl-carbodiimide and Na+ compete for binding to subunit c
N,N,N',N'-tetracyclohexyl-1,2-phenylenedioxydiacetamide
-
i.e. ETH 2120, complete inhibition. Addition of ETH 2120 to the assay during active transport of Na+ immediately stops further Na+ translocation into the lumen of the proteoliposomes
Venturicidin
-
inhibition of both ATPase and Na+ translocation activities
Cu2+
-
almost no ATPase activity is observed in the presence of CuCl2 or NiCl2
diethylstilbestrol
-
0.75 mM, almost complete inhibition. ATP-driven Na+ transport in proteoliposomes is also inhibited completely
N,N'-dicyclohexylcarbodiimide
-
inhibition of both ATPase and Na+ translocation activities, complete inhibition at 0.005 mM
N,N'-dicyclohexylcarbodiimide
-
inhibits in a pH dependent manner, binding covalently to acidic amino acid residues, inactivation is prevented by the presence of Na+ and Li+
N,N'-dicyclohexylcarbodiimide
-
wild type enzyme is inhibited mutant enzyme not
N,N'-dicyclohexylcarbodiimide
-
0.05 mM, at pH 7.0, 60% inhibition in the presence of 50 mM NaCl, no inhibitory effect in the presence of 1mM NaCl at pH 9.0
N-10-benzylamiloride
-
70% inhibition at 0.1 mM, Na+ protects against inactivation
Ni2+
-
almost no ATPase activity is observed in the presence of CuCl2 or NiCl2
additional information
-
in contrast with other V-type ATPases, the enzyme is not inhibited by N-ethylmaleimide
-
additional information
-
trans-stilbene does not inhibit ATP hydrolysis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5-di-tert-butyl-4-hydroxybenzylidenemalononitrile
-
i.e.SF 6847. Transport of Na+ is slightly stimulated, indicating that Na+ transport is electrogenic
ATP
-
ATP-induced stimulation of proximal tubule Na+-ATPase activity is mediated by a protein kinase C-dependent receptor P2Y2 and/or P2Y4 pathway
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Monkey cerebral arterial relaxation caused by hypercapnic acidosis and hypertonic bicarbonate.
Acidosis
Protection of reoxygenated cardiomyocytes against hypercontracture by inhibition of Na+/H+ exchange.
Atherosclerosis
Functional and histological changes in mesenteric arteries and aortas from monkeys fed a high cholesterol diet.
Cardiomegaly
Down-regulation of Na+ pump alpha 2 isoform in isoprenaline-induced cardiac hypertrophy in rat: evidence for increased receptor binding affinity but reduced inotropic potency of digoxin.
Cardiomegaly
Modulation by chronic nifedipine of plasma atrial natriuretic peptide, cell Na+ transport and plasma volume in rats with renal hypertension.
Cholera
Adenosine reverses the stimulatory effect of angiotensin II on the renal Na+-ATPase activity through the A2 receptor.
Cholera
Angiotensin II activates the ouabain-insensitive Na+-ATPase from renal proximal tubules through a G-protein.
Cholera
Effect of adenosine on the ouabain-insensitive Na+-ATPase activity from basolateral membrane of the proximal tubule.
Cholera
PKA-mediated effect of MAS receptor in counteracting angiotensin II-stimulated renal Na+-ATPase.
Cholera
Stimulation of the proximal tubule Na+-ATPase activity by adenosine A(2A) receptor.
Contracture
Effects of angiotensin II on intracellular calcium and contracture in metabolically inhibited cardiomyocytes.
Cystic Fibrosis
Inhibition of Na+,K+-ATPase by interferon gamma down-regulates intestinal epithelial transport and barrier function.
Dehydration
Resistance of mTAL Na+-dependent transporters and collecting duct aquaporins to dehydration in 7-month-old rats.
Heart Failure
Sarcolemmal Na(+)-K(+)-ATPase activity in congestive heart failure due to myocardial infarction.
Hyperglycemia
Differential stimulation of Na+ pump activity by insulin and nitric oxide in rabbit aorta.
Hypertension
A low concentration of ouabain (0.18 microg/kg) enhances hypertension in spontaneously hypertensive rats by inhibiting the Na+ pump and activating the renin-angiotensin system.
Hypertension
Chronic treatment with nifedipine prevents development of hypertension and abnormal red cell Na+ transport in Dahl-S-rats.
Hypertension
Effects of small doses of ouabain on the arterial blood pressure of anesthetized hypertensive and normotensive rats.
Hypertension
Modulation by chronic nifedipine of plasma atrial natriuretic peptide, cell Na+ transport and plasma volume in rats with renal hypertension.
Hypertension
Myocardial Na+-K+-ATPase activity and [3H]ouabain binding sites in hypertensive rats.
Hypertension
Regulation of renal ouabain-resistant Na+-ATPase by leptin, nitric oxide, reactive oxygen species, and cyclic nucleotides: implications for obesity-associated hypertension.
Hypertension
Renal molecular mechanisms underlying altered Na+ handling and genesis of hypertension during adulthood in prenatally undernourished rats.
Hypertension
Sodium pump activity and contraction of renal artery from spontaneously hypertensive rats.
Hypertension, Renal
Investigations on the Na+, K+-pump in erythrocytes of patients with renal hypertension.
Hypotension
Flow thresholds for cerebral energy disturbance and Na+ pump failure as studied by in vivo 31P and 23Na nuclear magnetic resonance spectroscopy.
Hypothyroidism
Permissive effect of thyroid hormones on induction of rat colonic Na+ transport by aldosterone is not localised at the level of Na+ channel transcription.
Leishmaniasis, Cutaneous
Anti-parasitic effect of the diuretic and Na+-ATPAse inhibitor furosemide in cutaneous leishmaniasis.
Microvascular Angina
Decreased activity of the red blood cell ATPase-dependent Na+ pump in patients with cardiac syndrome X.
Myocardial Infarction
Sarcolemmal Na(+)-K(+)-ATPase activity in congestive heart failure due to myocardial infarction.
Neoplasms
Equilibrium and steady-state models of the coupling between the amino acid gradient and the sodium electrochemical gradient in mouse ascites- tumour cells.
Neoplasms
Phosphorylation of the beta subunit of Na+K+-ATPase in Ehrlich ascites tumor by a membrane-bound protein kinase.
Neuroblastoma
Inhibition of Na+, K+-ATPase activates swelling-induced taurine efflux in a human neuroblastoma cell line.
Paralysis
[3H]ouabain binding in skeletal muscle from horses with hyperkalemic periodic paralysis.
Paralysis, Hyperkalemic Periodic
[3H]ouabain binding in skeletal muscle from horses with hyperkalemic periodic paralysis.
Pneumonia
The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane-bound subunits beta and gamma.
Renal Insufficiency, Chronic
Investigations on the Na+, K+-pump in erythrocytes of patients with renal hypertension.
Tuberculosis, Multidrug-Resistant
Bio-layer interferometry for measuring kinetics of protein-protein interactions and allosteric ligand effects.
Vaccinia
Translational regulation of Na,K-ATPase alpha1 and beta1 polypeptide expression in epithelial cells.
Virus Diseases
Inhibition of Na+K+ATPase activity in membranes of Sindbis virus-infected chick cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.5
-
enzyme from membrane vesicles, at 40°C in 50 mM MOPS buffer (pH 7.5.)
1.1
-
enzyme after 2.2fold purification, at 40°C in 50 mM MOPS buffer (pH 7.5)
15
-
enzyme after 30fold purification, at 40°C in 50 mM MOPS buffer (pH 7.5)
6
-
enzyme after 12fold purification, at 40°C in 50 mM MOPS buffer (pH 7.5)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
pH 5.0: about 20% of maximal activity, pH 5.5: about 85% of maximal activity, pH 9.0: abozt 55% of maximal activity
6.5 - 9.5
-
the enzyme exhibits Na+/H+ and K+/H+ antiport activity at a wide range of pH 7.0-9.5, but Li+/H+ antiport activity at pH between 7.5 and 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ntpA; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpA
SwissProt
brenda
gene ntpB; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpB
SwissProt
brenda
gene ntpC; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpC
SwissProt
brenda
gene ntpD; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpD
SwissProt
brenda
gene ntpE; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpE
SwissProt
brenda
gene ntpF; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpF
SwissProt
brenda
gene ntpG; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpG
SwissProt
brenda
gene ntpI; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpI
SwissProt
brenda
gene ntpK; strain ATCC 43024, ntpFIKECGABD operon contains the structural genes coding for the nine subunits of the enzyme complex, gene ntpK
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
brenda
-
the enzyme is orientated to the cytoplasmic side, structural model of V-ATPase, overview
brenda
-
brenda
Show AA Sequence and Transmembrane Helices (321 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
x * 10000, G subunit, SDS-PAGE, x * 11600, about, G subunit, sequence calculation
100000
11000
11409
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
11600
x * 10000, G subunit, SDS-PAGE, x * 11600, about, G subunit, sequence calculation
12000
x * 12000, F subunit, SDS-PAGE, x * 12300, about, F subunit, sequence calculation
12300
x * 12000, F subunit, SDS-PAGE, x * 12300, about, F subunit, sequence calculation
14000
14184
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
14255
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
15000
16000
16036
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
17000
x * 17000, K subunit, SDS-PAGE, x * 17600, about, K subunit, sequence calculation
17600
x * 17000, K subunit, SDS-PAGE, x * 17600, about, K subunit, sequence calculation
19000
19443
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
20763
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
22699
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
22700
x * 26000, E subunit, SDS-PAGE, x * 22700, about, E subunit, sequence calculation
23000
24000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
24300
x * 25500, D subunit, SDS-PAGE, x * 24300, about, D subunit, sequence calculation
25447
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
25500
x * 25500, D subunit, SDS-PAGE, x * 24300, about, D subunit, sequence calculation
26000
x * 26000, E subunit, SDS-PAGE, x * 22700, about, E subunit, sequence calculation
27000
27093
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
31709
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
35000
37000
x * 37000, C subunit, SDS-PAGE, x * 38400, about, C subunit, sequence calculation
38000
38162
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
38400
x * 37000, C subunit, SDS-PAGE, x * 38400, about, C subunit, sequence calculation
400000
48869
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
50453
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
51000
51139
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
51200
x * 51000, B subunit, SDS-PAGE, x * 51200, about, B subunit, sequence calculation
52000
55667
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
57000
65000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
65766
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
66000
69000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
7164
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
72300
x * 72300, I subunit, SDS-PAGE, x * 72300, about, I subunit, sequence calculation
75619
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
76000
8000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
8255
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
11000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
11000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
14000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
14000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
14000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
15000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
15000
-
x * 4800 + x * 15000 + x * 19000 + x * 35000 + x * 52000 + x * 57000, at least 6 subunits, SDS-PAGE
16000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
16000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
16000
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
19000
-
x * 4800 + x * 15000 + x * 19000 + x * 35000 + x * 52000 + x * 57000, at least 6 subunits, SDS-PAGE
19000
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
23000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
23000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
27000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
27000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
27000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
35000
-
x * 4800 + x * 15000 + x * 19000 + x * 35000 + x * 52000 + x * 57000, at least 6 subunits, SDS-PAGE
35000
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
38000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
38000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
38000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
51000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
51000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
51000
x * 51000, B subunit, SDS-PAGE, x * 51200, about, B subunit, sequence calculation
52000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
52000
-
x * 4800 + x * 15000 + x * 19000 + x * 35000 + x * 52000 + x * 57000, at least 6 subunits, SDS-PAGE
52000
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
57000
-
x * 4800 + x * 15000 + x * 19000 + x * 35000 + x * 52000 + x * 57000, at least 6 subunits, SDS-PAGE
57000
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
66000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
66000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
66000
x * 66000, A subunit, SDS-PAGE, x * 66000, about, A subunit, sequence calculation
76000
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
76000
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
homotetramer
multimer
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
nonamer
oligomer
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
additional information
?
-
x * 4800 + x * 15000 + x * 19000 + x * 35000 + x * 52000 + x * 57000, at least 6 subunits, SDS-PAGE
?
x * 10000, G subunit, SDS-PAGE, x * 11600, about, G subunit, sequence calculation
?
x * 12000, F subunit, SDS-PAGE, x * 12300, about, F subunit, sequence calculation
?
x * 17000, K subunit, SDS-PAGE, x * 17600, about, K subunit, sequence calculation
?
x * 25500, D subunit, SDS-PAGE, x * 24300, about, D subunit, sequence calculation
?
x * 26000, E subunit, SDS-PAGE, x * 22700, about, E subunit, sequence calculation
?
x * 37000, C subunit, SDS-PAGE, x * 38400, about, C subunit, sequence calculation
?
x * 51000, B subunit, SDS-PAGE, x * 51200, about, B subunit, sequence calculation
?
x * 66000, A subunit, SDS-PAGE, x * 66000, about, A subunit, sequence calculation
?
x * 72300, I subunit, SDS-PAGE, x * 72300, about, I subunit, sequence calculation
?
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
?
-
x * 66000, subunitA, + x * 51000, subunit B, + x * 76000, subunit I, + x * 38000, subunit C, + x * 27000, subunit D, + x * 23000, subunit E, + x * 16000, subunit K, + x * 14000, subunit F, + x * 11000, subunit G
?
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
nonamer
-
the c subunit determines the ion specificity of the ATP synthases/ATPases (Na+-transporting or H+-transporting). Calculated from sequence, the c subunit has a molecular mass of 16061 Da with four transmembrane helices
nonamer
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
-
the enzyme complex consists of an integral membrane part V0 and a cytoplasmic, membrane-associated part V1, V0 is built of subunits K and I, V1 consists of seven subunits, termed A, B, C, D, E, F, and G, to determine the identity of the proteins in two pairs of subunits, the nine subunits of the enzyme complex are separated by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides
additional information
-
the peripheral stalk of Na+-translocating V-ATPase of Enterococcus hirae is composed of NtpE and NtpF subunits together with the N-terminal hydrophilic domain of NtpI, structural model of V-ATPase, overview. Subunit interaction analysis by pulldown assay and surface plasmon resonance, detailed overview
additional information
-
hypothetical model of the subunit topology of A1AO ATP synthases: subunits a and c form the membrane-embedded motor, with a being the stator, and multiple copies of subunit c forming the rotor. The rotor subunit c forms an SDS-resistant oligomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
phosphorylation of this protein requires the presence of Na+, while other alkali cations (K+, Li+, Rb+) are ineffective
phosphoprotein
-
phosphorylation of this protein requires the presence of Na+, while other alkali cations (K+, Li+, Rb+) are ineffective
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
0.005 ml of 2 mg/ml purified K-ring in 20 mM Tris-HCl, pH 7.5, 100 mM LiCl, 10% glycerol, and 0.32 mM n-dodecyl-beta-D-maltoside by sitting drop vapor diffusion method, mixing with 0.005 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, 4% glycerol, 240 mM potassium citrate, 1.2 mM undecylmaltoside, and 34% PEG 400, at 20°C, in presence or absence of 10 mM NaCl, first appearance after 3 days, maximal size after 3 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A236C
A214C
-
N-ethylmaleimide significantly inhibits ATP synthesis (18%) and hydrolysis as well as proton pumping activities of the enzyme
A218C
-
N-ethylmaleimide significantly inhibits ATP synthesis (19%) and hydrolysis as well as proton pumping activities of the enzyme
F217C
-
the mutant shows wild type activity also in the presence of N-ethylmaleimide
G215C
-
N-ethylmaleimide significantly inhibits ATP synthesis (42%) and hydrolysis as well as proton pumping activities of the enzyme
I223C
-
N-ethylmaleimide significantly inhibits ATP synthesis (45%) and hydrolysis as well as proton pumping activities of the enzyme
K219C
-
N-ethylmaleimide significantly inhibits ATP synthesis activity (43%) of the enzyme
N222C
-
N-ethylmaleimide significantly inhibits ATP synthesis and hydrolysis as well as proton pumping activities of the enzyme
N230C
-
N-ethylmaleimide significantly inhibits ATP synthesis (38%) and hydrolysis as well as proton pumping activities of the enzyme
P220C
-
the mutant shows about wild type activity also in the presence of N-ethylmaleimide
T221C
-
N-ethylmaleimide significantly inhibits ATP synthesis and hydrolysis as well as proton pumping activities of the enzyme
additional information
-
mutant with a lesion in membrane Na+-translocation is neither inhibited by dicyclohexylcarbodiimide nor stimulated by Na+
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
without glycerol, the purified enzyme, 1 mg/ml in 50 mM Tris-HCl, pH 7.5 is inactivated by overnight exposure to 4°C
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 10 mM Tris-HCl pH 8.0 containing 2 mM MgCl2 to a protein concentration of 1.5 mg/ml, stable for at least 2 months
-
4°C, 50 mM MOPS pH 7.5, 4 days, no activity loss of the native enzyme
-
4°C, 50 mM MOPS pH 7.5, 5 days, 75% activity loss of the purified enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the V-ATPase and isolation of the K-ring by by anion exchange chromatography and gel filtration
-
separate purification of His-tagged NtpE and NtpF, and His-tagged N-terminal hydrophilic domain of NtpI by nickel affinity and ion exchange chromatography, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes ntpE and ntpF encoding the two subunits of the enzyme, expression of both subunits and the N-terminal soluble domain of NtpI as His-tagged proteins in Escherichia coli strain BL21(DE3)
-
ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the activity of Na+-ATPase is increased in rats receiving weekly hydrodynamic injection (1 mg/kg) of a naked plasmid containing human HGF gene associated with a cytomegalovirus promoter during 6 weeks
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takase, K.; Yamato, I.; Igarashi, K.; Kakinuma, Y.
Indespensable glutamic acid residue-139 of NtpK proteolipid in the reaction of vacuolar Na+-translocating ATPase in Enterococcus hirae
Biosci. Biotechnol. Biochem.
63
1125-1129
1999
Enterococcus hirae
brenda
Takase, K.; Kakinuma, S.; Yamato, I.; Konishi, K.; Igarashi, K.; Kakinuma, Y.
Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae
J. Biol. Chem.
269
11037-11044
1994
Enterococcus hirae
brenda
Solioz, M.; Davies, K.
Operon of vacuolar-type Na+-ATPase of Enterococcus hirae
J. Biol. Chem.
269
9453-9459
1994
Enterococcus hirae
brenda
Rahlfs, S.; Muller, V.
Sequence of subunit c of the Na+-translocating F1F0 ATPase of Acetobacterium woodii: proposal for determinats of Na+ specificity as revealed by sequence comparison
FEBS Lett.
404
269-271
1997
Acetobacterium woodii
brenda
Forster, A.; Daniel, R.; Muller, V.
The Na+-translocating ATPase of Acetobacterium woodii is a F1F0-type enzyme as deduced from the primary structure of its beta, gamma and epsilon subunits
Biochim. Biophys. Acta
1229
393-397
1995
Acetobacterium woodii
brenda
Murata, T.; Igarashi, K.; Kakinuma, Y.; Yamato, I.
Na+ binding of V-type Na+-ATPase in Enterococcus hirae
J. Biol. Chem.
275
13415-13419
2000
Enterococcus hirae
brenda
Murata, T.; Takase, K.; Yamato, I.; Igarashi, K.; Kakinuma, Y.
Purification and reconstitution of Na+-translocating vacuolar ATPase from Enterococcus hirae
J. Biol. Chem.
272
24885-24890
1997
Enterococcus hirae
brenda
Kluge, C.; Dimroth, P.
Studies on Na+ and H+ translocation through the F0 part of the Na+-translocating F1F0 ATPase from Propionibacterium modestum: discovery of a membrane potential dependent step
Biochemistry
31
12665-12672
1992
Propionigenium modestum
brenda
Kakinuma, Y.; Yamato, I.; Murata, T.
Structure and function of vacuolar Na+-translocating ATPase in Enterococcus hirae
J. Bioenerg. Biomembr.
31
7-14
1999
Enterococcus hirae
brenda
Murata, T.; Yamato, I.; Igarashi, K.; Kakinuma, Y.
Intracellular Na+ regulates transcription of the ntp operon encoding a vacuolar-type Na+-translocating ATPase in Enterococcus hirae
J. Biol. Chem.
271
23661-23666
1996
Enterococcus hirae
brenda
Kakinuma, Y.; Igarashi, K.
Purification and characterization of the catalytic moiety of vacuolar-type Na+-ATPase from Enterococcus hirae
J. Biochem.
116
1302-1308
1994
Enterococcus hirae
brenda
Smigan, P.; Polak, P.; Majernik, A.; Greksak, M.
Isolation and characterization of a neomycin-resistant mutant of Methanobacterium thermoautotrophicum with a lesion in Na+-translocating ATPase (synthase)
FEBS Lett.
420
93-96
1997
Methanothermobacter thermautotrophicus
brenda
Reidlinger, J.; Muller, V.
Purification of ATP synthase from Acetobacterium woodii and identification as a Na+-translocating F1F0-type enzyme
Eur. J. Biochem.
223
275-283
1994
Acetobacterium woodii
brenda
Smigan, P.; Majernik, A.; Polak, P.; Hapala, I.; Greksak, M.
The presence of H+ and Na+-translocating ATPases in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions
FEBS Lett.
371
119-122
1995
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH
brenda
Muller, V.; Aufurth, S.; Rahlfs, S.
The Na(+) cycle in Acetobacterium woodii: identification and characterization of a Na(+) translocating F(1)F(0)-ATPase with a mixed oligomer of 8 and 16 kDa proteolipids
Biochim. Biophys. Acta
1505
108-120
2001
Acetobacterium woodii
brenda
Murata, T.; Kawano, M.; Igarashi, K.; Yamato, I.; Kakinuma, Y.
Catalytic properties of Na(+)-translocating V-ATPase in Enterococcus hirae
Biochim. Biophys. Acta
1505
75-81
2001
Enterococcus hirae
brenda
Murata, T.; Yoshikawa, Y.; Hosaka, T.; Takase, K.; Kakinuma, Y.; Yamato, I.; Kikuchi, T.
Nucleotide-binding sites in V-type Na+-ATPase from Enterococcus hirae
J. Biochem.
132(5)
789-794
2002
Enterococcus hirae
brenda
Kawano, M.; Igarashi, K.; Yamato, I.; Kakinuma, Y.
Arginine residue at position 573 in Enterococcus hirae vacuolar-type ATPase NtpI subunit plays a crucial role in Na+ translocation
J. Biol. Chem.
277
24405-24410
2002
Enterococcus hirae
brenda
Popova, L.G.; Shumkova, G.A.; Andreev, I.M.; Balnokin, Y.V.
Functional identification of electrogenic Na+-translocating ATPase in the plasma membrane of the halotolerant microalga Dunaliella maritima
FEBS Lett.
579
5002-5006
2005
Dunaliella maritima
brenda
Ferguson Scott, F.S.; Keis Stefani, K.S.; Cook Gregory, C.G.
Biochemical and molecular characterization of a Na+-translocating F1Fo-ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum
J. Bacteriol.
188
5045-5054
2006
[Clostridium] paradoxum
brenda
Murata, T.; Yamato, I.; Kakinuma, Y.
Structure and mechanism of vacuolar Na+-translocating ATPase from Enterococcus hirae
J. Bioenerg. Biomembr.
37
411-413
2005
Enterococcus hirae
brenda
Balnokin, Y.V.; Popova, L.G.; Pagis, L.Y.; Andreev, I.M.
The Na+-translocating ATPase in the plasma membrane of the marine microalga Tetraselmis viridis catalyzes Na+/H+ exchange
Planta
219
332-337
2004
Tetraselmis viridis
brenda
Murata, T.; Yamato, I.; Kakinuma, Y.; Leslie, A.G.; Walker, J.E.
Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae
Science
308
654-659
2005
Enterococcus hirae
brenda
Ubbink-Kok, T.; Nijland, J.; Slotboom, D.J.; Lolkema, J.S.
The ntp operon encoding the Na+ V-ATPase of the thermophile Caloramator fervidus
Arch. Microbiol.
186
513-517
2006
Caloramator fervidus (Q2EQR4), Caloramator fervidus (Q2EQR5), Caloramator fervidus (Q2EQR6), Caloramator fervidus (Q2EQR7), Caloramator fervidus (Q2EQR8), Caloramator fervidus (Q2EQR9), Caloramator fervidus (Q2EQS0), Caloramator fervidus (Q2EQS1), Caloramator fervidus (Q2EQS2), Caloramator fervidus
brenda
Yamamoto, M.; Unzai, S.; Saijo, S.; Ito, K.; Mizutani, K.; Suno-Ikeda, C.; Yabuki-Miyata, Y.; Terada, T.; Toyama, M.; Shirouzu, M.; Kobayashi, T.; Kakinuma, Y.; Yamato, I.; Yokoyama, S.; Iwata, S.; Murata, T.
Interaction and stoichiometry of the peripheral stalk subunits NtpE and NtpF and the N-terminal hydrophilic domain of NtpI of Enterococcus hirae V-ATPase
J. Biol. Chem.
283
19422-19431
2008
Enterococcus hirae
brenda
Murata, T.; Yamato, I.; Kakinuma, Y.; Shirouzu, M.; Walker, J.E.; Yokoyama, S.; Iwata, S.
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase
Proc. Natl. Acad. Sci. USA
105
8607-8612
2008
Enterococcus hirae
brenda
Pisa, K.Y.; Huber, H.; Thomm, M.; Mueller, V.
A sodium ion-dependent A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus
FEBS J.
274
3928-3938
2007
Pyrococcus furiosus
brenda
Wengert, M.; Ribeiro, M.C.; Abreu, T.P.; Coutinho-Silva, R.; Leao-Ferreira, L.R.; Pinheiro, A.A.; Caruso-Neves, C.
Protein kinase C-mediated ATP stimulation of Na(+)-ATPase activity in LLC-PK1 cells involves a P2Y2 and/or P2Y4 receptor
Arch. Biochem. Biophys.
535
136-142
2013
Sus scrofa
brenda
Mayer, F.; Lim, J.K.; Langer, J.D.; Kang, S.G.; Mller, V.
Na+ transport by the A1AO ATP synthase purified from Thermococcus onnurineus and reconstituted into liposomes
J. Biol. Chem.
290
6994-7002
2015
Thermococcus onnurineus
brenda
Romero-Vasquez, F.; Chavez, M.; Perez, M.; Arcaya, J.; Garcia, A.; Rincon, J.; Rodriguez-Iturbe, B.
Overexpression of HGF transgene attenuates renal inflammatory mediators, Na+-ATPase activity and hypertension in spontaneously hypertensive rats
Biochim. Biophys. Acta
1822
1590-1599
2012
Rattus norvegicus
brenda
Kishimoto, M.; Shimajiri, Y.; Oshima, A.; Hase, A.; Mikami, K.; Akama, K.
Functional expression of an animal type-Na+-ATPase gene from a marine red seaweed Porphyra yezoensis increases salinity tolerance in rice plants
Plant Biotechnol.
30
417-422
2013
Neopyropia yezoensis (Q4LB57)
-
brenda
Popova, L.; Balnokin, Y.
Na+-ATPases of halotolerant microalgae
Russ. J. Plant Physiol.
60
472-482
2013
Tetraselmis viridis, Dunaliella maritima
-
brenda
Mitome, N.; Sato, H.; Tomiyama, T.; Shimabukuro, K.; Matsunishi, T.; Hamada, K.; Suzuki, T.
Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo-alpha subunit of Propionigenium modestum ATP synthase
Biophys. Physicobiol.
14
41-47
2017
Propionigenium modestum
brenda
Meng, L.; Meng, F.; Zhang, R.; Zhang, Z.; Dong, P.; Sun, K.; Chen, J.; Zhang, W.; Yan, M.; Li, J.; Abdel-Motaal, H.; Jiang, J.
Characterization of a novel two-component Na+(Li+, K+)/H+ antiporter from Halomonas zhaodongensis
Sci. Rep.
7
4221
2017
Halomonas zhaodongensis, Halomonas zhaodongensis NEAU-ST10-25T
brenda
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