Literature summary for 3.6.4.B6 extracted from

Ghosh, A.; Hartung, S.; van der Does, C.; Tainer, J.A.; Albers, S.V.
Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding (2011), Biochem. J., 437, 43-52.

Search for more literature for 3.6.4.B6

Activating Compound

Activating Compound	Comment	Organism	Structure
Sulfolobus acidocaldarius tetraether lipid	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	Sulfolobus acidocaldarius

Cloned(Commentary)

Cloned (Comment)	Organism
expression of histidine-tagged and wild-type enzyme in Escherichia coli	Sulfolobus acidocaldarius

Protein Variants

Protein Variants	Comment	Organism
D290A	mutation has no effect on ATP hydrolysis	Sulfolobus acidocaldarius
E336A	mutation results in a reduction of approximately 90% of ATP hydrolysis compared with wild-type enzyme, mutant forms a stable oligomer after ATP binding	Sulfolobus acidocaldarius
K268A	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	Sulfolobus acidocaldarius

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	preferred divalent cation for ATP hydrolysis. Considerable activity is detected in the presence of Ca2+ and Mg2+ respectively	Sulfolobus acidocaldarius
Mg2+	preferred divalent cation for ATP hydrolysis. Considerable activity is detected in the presence of Ca2+ and Mg2+ respectively	Sulfolobus acidocaldarius
Mn2+	preferred divalent cation for ATP hydrolysis. Considerable activity is detected in the presence of Ca2+ and Mg2+ respectively	Sulfolobus acidocaldarius

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
55000	-	6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration	Sulfolobus acidocaldarius
330000	-	gel filtration	Sulfolobus acidocaldarius

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Sulfolobus acidocaldarius	it is proposed that the enzyme is bi-functional in driving flagella assembly and movement	ADP + phosphate	-	?
ATP + H2O	Sulfolobus acidocaldarius DSM 639	it is proposed that the enzyme is bi-functional in driving flagella assembly and movement	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Sulfolobus acidocaldarius	Q4J9L0	-	-
Sulfolobus acidocaldarius DSM 639	Q4J9L0	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sulfolobus acidocaldarius

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + H2O = ADP + phosphate	it is proposed that the enzyme is bi-functional in driving flagella assembly and movement	Sulfolobus acidocaldarius	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	it is proposed that the enzyme is bi-functional in driving flagella assembly and movement	Sulfolobus acidocaldarius	ADP + phosphate	-	?
ATP + H2O	hydrolyses ATP in a co-operative manner. Hydrolyses ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP. No conversion of ADP into AMP is detected	Sulfolobus acidocaldarius	ADP + phosphate	-	?
ATP + H2O	it is proposed that the enzyme is bi-functional in driving flagella assembly and movement	Sulfolobus acidocaldarius DSM 639	ADP + phosphate	-	?
ATP + H2O	hydrolyses ATP in a co-operative manner. Hydrolyses ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP. No conversion of ADP into AMP is detected	Sulfolobus acidocaldarius DSM 639	ADP + phosphate	-	?
CTP + H2O	hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP	Sulfolobus acidocaldarius	CDP + phosphate	-	?
CTP + H2O	hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP	Sulfolobus acidocaldarius DSM 639	CDP + phosphate	-	?
GTP + H2O	hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP	Sulfolobus acidocaldarius	GDP + phosphate	-	?
GTP + H2O	hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP	Sulfolobus acidocaldarius DSM 639	GDP + phosphate	-	?
UTP + H2O	hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP	Sulfolobus acidocaldarius	UDP + phosphate	-	?
UTP + H2O	hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP	Sulfolobus acidocaldarius DSM 639	UDP + phosphate	-	?

Subunits

Subunits	Comment	Organism
hexamer	6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration	Sulfolobus acidocaldarius

Synonyms

Synonyms	Comment	Organism
FlaI	-	Sulfolobus acidocaldarius
Saci_1173	locus name	Sulfolobus acidocaldarius

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
75	-	-	Sulfolobus acidocaldarius

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
70	80	70°C: about 50% of maximal activity, 80°C: 25% of maximal activity	Sulfolobus acidocaldarius

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	-	-	Sulfolobus acidocaldarius

pH Range

pH Minimum	pH Maximum	Comment	Organism
4	8	pH 4.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity	Sulfolobus acidocaldarius

General Information

General Information	Comment	Organism
physiological function	it is proposed that the enzyme is bi-functional in driving flagella assembly and movement	Sulfolobus acidocaldarius

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Release 2023.1 (January 2023)