Cloned (Comment) | Organism |
---|---|
expression of FoF1, tagged with His10 at the beta-subunit N-terminus, in Escherichia coli strain DK8 | Bacillus sp. PS3 |
Protein Variants | Comment | Organism |
---|---|---|
alphaR169A | thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1 | Bacillus sp. PS3 |
alphaR169E | thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1 | Bacillus sp. PS3 |
alphaR169G/Q217R | substitutions in the gamma subunit of Fo, the mutation blocks the passive proton translocation | Bacillus sp. PS3 |
alphaR169X | thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation | Bacillus sp. PS3 |
gammaE56Q | substitution of Glu56 in the gamma subunit of Fo, the mutation blocks the passive proton translocation | Bacillus sp. PS3 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Bacillus sp. PS3 | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Bacillus sp. PS3 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + H+/out | Bacillus sp. PS3 | - |
ATP + H2O + H+/in | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus sp. PS3 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His10-tagged FoF1, from Echerichia coli strain DK8 by nickel affinity chromatography | Bacillus sp. PS3 |
Renatured (Comment) | Organism |
---|---|
stripping of F1 and Fo from recombinant membrane fragments, and functional purified FoF1s reconstitutions in proteoliposomes, suspended in 10 mM HEPES/NaOH, pH 7.5, 0.25 M sucrose, and 5 mM MgSO4, at 25°C | Bacillus sp. PS3 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphate + H+/out | - |
Bacillus sp. PS3 | ATP + H2O + H+/in | - |
r | |
additional information | an essential arginine residue R169 of the Fo-alpha subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel, overview | Bacillus sp. PS3 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FoF1 | - |
Bacillus sp. PS3 |
FoF1-ATP synthase | - |
Bacillus sp. PS3 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
ATPase assay at | Bacillus sp. PS3 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
ATPase assay at | Bacillus sp. PS3 |