Article
Identification of the magnesium-binding domain of the high-affinity ATP-binding site of the Bacillus subtilis and Escherichia coli SecA protein.
The Journal of biological chemistry - 11 Aug 1995
van der Wolk J P, Klose M, de Wit J G, den Blaauwen T, Freudl R, Driessen A J
Abstract excerpt
The homodimeric SecA protein is the peripheral subunit of the translocase, and couples the hydrolysis of ATP to the translocation of precursor proteins across the bacterial cytoplasmic membrane. The high affinity ATP binding activity of SecA resides in the amino-terminal domain of SecA. This domain contains a tandem repeat of the "so-called" Walker B-motif, hXhhD (Walker, J.E., Saraste, M., Runswick, M.J., and...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Bacillus subtilis
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Escherichia coli
- Escherichia coli Proteins
- Magnesium