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Information on EC 7.1.2.2 - H+-transporting two-sector ATPase

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EC Tree
IUBMB Comments
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9--12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
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UNIPROT: Q0ZS23
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
atp synthase, v-atpase, f1-atpase, h+-atpase, mitochondrial atpase, vacuolar h(+)-atpase, vacuolar atpase, lipid-binding protein, vacuolar h+-atpase, f0f1-atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F1FO-ATP synthase
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15 kDa mediatophore protein
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32 kDa accessory protein
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59 kDa membrane-associated GTP-binding protein
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-
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A6L
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-
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ATP synthase
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-
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ATP synthase proteolipid P1
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ATP synthase proteolipid P2
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-
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ATP synthase proteolipid P3
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bacterial Ca2+/Mg2+ ATPase
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-
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BN59
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C7-1 protein
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CGI-11
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-
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chloroplast ATPase
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-
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coupling factors (F0,F1 and CF1)
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-
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Dicyclohexylcarbodiimide-binding protein
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-
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Ductin
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-
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DVA41
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F0F1-ATPase
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F1-ATPase
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-
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F1F0 ATPase
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-
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F1F0H+-ATPase
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-
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H+-ATPase
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H+-translocating ATPase
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-
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H+-transporting ATPase
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HATPL
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-
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HO57
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-
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Invasion protein invC
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-
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Isoform HO68
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Isoform VA68
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Lipid-binding protein
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M40
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-
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mitochondrial ATPase
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My032 protein
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Oligomycin sensitivity conferral protein
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-
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OSCP
-
-
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P31
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-
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P39
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Physophilin
-
-
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PKIWI505
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Protein bellwether
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Sul-ATPase alpha
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-
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Sul-ATPase beta
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-
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SUL-ATPase epsilon
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-
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Sul-ATPase gamma
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-
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UV-inducible PU4 protein
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V-ATPase 28 kDa accessory protein
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V-ATPase 40 kDa accessory protein
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V-ATPase 41 KDa accessory protein
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V-ATPase 9.2 kDa membrane accessory protein
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V-ATPase S1 accessory protein
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VEG100
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VEG31
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Vegetative protein 100
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Vegetative protein 31
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VHA16K
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YOPS secretion ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-transporting)
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9--12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + H+
ATP + H2O
show the reaction diagram
low rates of ATP synthesis
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
can function in place of MgCl2, although the affinity is much lower
Na+
stimulates purified enzyme 3-4fold at pH 7.0 or 5-6fold at pH 9.0 with increasing concentrations of Na+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N,N'-dicyclohexylcarbodiimide
0.2 mM can inhibit over 70% of activity after 20 min, which is pH dependent, 50 mM NaCl provides 40% protection against inhibition at pH 7.0, at pH 9.0 1 mM NaCl protects 100%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 1
ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
enzyme retains ca. 20% of its maximum activity at below pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM7308
SwissProt
Manually annotated by BRENDA team
strain DSM7308
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATPF_CLOPD
169
0
19444
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
stable for 4 days, retaining near 100% of the starting activity, in contrast, the purified enzyme rapidly loses activity overnight and retains only 25% of its starting activity after 5 days
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
30fold by cholate washed vesicles followed by Triton X-100 solubilization and PEG 6000 precipitation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
F1FO-ATP synthase is a Na+-translocating ATPase used to generate an electrochemical gradient of Na+ that can drive other membrane-bound bioenergetic processes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q0ZS18), [Clostridium] paradoxum (Q0ZS19), [Clostridium] paradoxum (Q0ZS20), [Clostridium] paradoxum (Q0ZS21), [Clostridium] paradoxum (Q0ZS22), [Clostridium] paradoxum (Q0ZS23), [Clostridium] paradoxum (Q0ZS24), [Clostridium] paradoxum (Q0ZS25), [Clostridium] paradoxum (Q0ZS26), [Clostridium] paradoxum, [Clostridium] paradoxum DSM 7308 (Q0ZS18), [Clostridium] paradoxum DSM 7308 (Q0ZS19), [Clostridium] paradoxum DSM 7308 (Q0ZS20), [Clostridium] paradoxum DSM 7308 (Q0ZS21), [Clostridium] paradoxum DSM 7308 (Q0ZS22), [Clostridium] paradoxum DSM 7308 (Q0ZS23), [Clostridium] paradoxum DSM 7308 (Q0ZS24), [Clostridium] paradoxum DSM 7308 (Q0ZS25), [Clostridium] paradoxum DSM 7308 (Q0ZS26)
Manually annotated by BRENDA team