Information on EC 3.6.4.B6 - archaeal flagellar ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.4.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
archaeal flagellar ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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
CTP + H2O
CDP + phosphate
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
UTP + H2O
UDP + phosphate
show the reaction diagram
additional information
?
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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
ADP + phosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sulfolobus acidocaldarius tetraether lipid
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tetraether lipids increases the ATPase activity 34-fold, whereas the addition of an Escherichia coli total lipid extract leads to a 1.5-fold stimulation of the ATPase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
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pH 4.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 80
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70C: about 50% of maximal activity, 80C: 25% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration
330000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FlaI can be purified from the cytoplasm of Escherichia coli
recombinant Strep II-tagged FlaI, Strep II-tagged FlaXc, and His6-tagged FlaH from in Escherichia coli strain BL21-CodonPlus-RIL as ternary complex by nickel affinity chromatography, or single FlaI by avidin affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of histidine-tagged and wild-type enzyme in Escherichia coli
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recombinant expression of Strep II-tagged FlaI protein in Escherichia coli strain BL21-CodonPlus-RIL, co-expression with Strep II-tagged FlaXc and His6-tagged FlaH
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the enzyme is encoded in the fla operon
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
FlaI mRNAS can be found only in stationary growth phase of arabinose- and maltose-grown cells. NO expression in media containing glucose or tryptone as sole carbon source
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D290A
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mutation has no effect on ATP hydrolysis
DELTA1-224
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in strains expressing the mutant enzyme no archaellum is assembled and swimming motility is abolished. Mutant enzyme still exhibits 75% of ATPase activity compared to the full-length FlaI
DELTA1-29
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strains overexpressing FlaIDELTA129 show that 10%20% of the cell population can assemble archaella, whereas complementation with wild-type FlaI leads to 40%50% of cells having archaella
E336A
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mutation results in a reduction of approximately 90% of ATP hydrolysis compared with wild-type enzyme, mutant forms a stable oligomer after ATP binding
K268A
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mutation results in a reduction of approximately 50% of ATP hydrolysis compared with wild-type enzyme, 20-fold lower binding affinity of ATP, no oligomerization
M69E/I72E/F76E
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localization to the membrane is significantly reduced compared to that of wild-type
D290A
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mutation has no effect on ATP hydrolysis
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DELTA1-224
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in strains expressing the mutant enzyme no archaellum is assembled and swimming motility is abolished. Mutant enzyme still exhibits 75% of ATPase activity compared to the full-length FlaI
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DELTA1-29
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strains overexpressing FlaIDELTA129 show that 10%20% of the cell population can assemble archaella, whereas complementation with wild-type FlaI leads to 40%50% of cells having archaella
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E336A
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mutation results in a reduction of approximately 90% of ATP hydrolysis compared with wild-type enzyme, mutant forms a stable oligomer after ATP binding
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K268A
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mutation results in a reduction of approximately 50% of ATP hydrolysis compared with wild-type enzyme, 20-fold lower binding affinity of ATP, no oligomerization
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M69E/I72E/F76E
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localization to the membrane is significantly reduced compared to that of wild-type
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additional information