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Literature summary for 7.6.2.9 extracted from
- Monitoring conformational changes during the catalytic cycle of OpuAA, the ATPase subunit of the ABC transporter OpuA from Bacillus subtilis (2008), Biochem. J., 412, 233-244.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli, cysteine mutants generated and inserted into pBAD33 | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F19W | mutant analyzed | Bacillus subtilis |
| G161C | single cysteine mutants generated by site-directed mutagenesis | Bacillus subtilis |
| S171C | single cysteine mutants generated by site-directed mutagenesis | Bacillus subtilis |
| S45C | single cysteine mutants generated by site-directed mutagenesis | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.6 | - |
ATP | wild-type, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis |  |
| 0.7 | - |
ATP | mutant S45C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis | |
| 1.7 | - |
ATP | mutant F19W, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis | |
| 2.8 | - |
ATP | mutant G161C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form | Bacillus subtilis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Bacillus subtilis | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P46920 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| gel filtration | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
studies on architecture and potential roles of the C-terminal accessory domain in structural and functional protein regulation performed, conformational changes during the catalytic cycle of the ATPase unit of OpuA protein determined, single cysteine mutants generated, static and time-resolved FRET measurements applied, molecular modelling and structural analysis shown | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Bacillus subtilis | ADP + phosphate | - |
? | |
| ATP + H2O | ATPase activity of monomeric OpuA protein measured in wild-type and single cysteine mutants, structural information on the architecture of the OpuA-ATPase by application of FRET techniques, C-terminal catalytic domain, helical domain and accessory domain analyzed | Bacillus subtilis | ADP + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OpuA | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at | Bacillus subtilis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 24 | assay at | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Bacillus subtilis |
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