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 (Comment) | Organism |
---|---|
expression of histidine-tagged and wild-type enzyme in Escherichia coli | Sulfolobus acidocaldarius |
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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration | Sulfolobus acidocaldarius |
330000 | - |
gel filtration | Sulfolobus acidocaldarius |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus acidocaldarius | Q4J9L0 | - |
- |
Sulfolobus acidocaldarius DSM 639 | Q4J9L0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Sulfolobus acidocaldarius |
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 |
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 | Comment | Organism |
---|---|---|
hexamer | 6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration | Sulfolobus acidocaldarius |
Synonyms | Comment | Organism |
---|---|---|
FlaI | - |
Sulfolobus acidocaldarius |
Saci_1173 | locus name | Sulfolobus acidocaldarius |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
75 | - |
- |
Sulfolobus acidocaldarius |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Sulfolobus acidocaldarius |
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 | Comment | Organism |
---|---|---|
physiological function | it is proposed that the enzyme is bi-functional in driving flagella assembly and movement | Sulfolobus acidocaldarius |