Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo

The SecA protein is a major component of the cellular machinery that mediates the translocation of proteins across the Escherichia coli plasma membrane. The secA gene from Bacillus subtilis was cloned and expressed in E. coli under the control of the lac or trc promoter. The temperature-sensitive gr...

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Veröffentlicht in:	The Journal of biological chemistry 1993-02, Vol.268 (6), p.4504-4510
Hauptverfasser:	KLOSE, M, SCHIMZ, K.-L, VAN DER WOLK, J, DRIESSEN, A. J. M, FREUDL, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Amino Acid Sequence ATP Bacillus subtilis Bacillus subtilis - genetics Bacillus subtilis - metabolism Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence binding Binding Sites Biological and medical sciences Biological Transport Catalysis Cell physiology complementation DNA, Bacterial Escherichia coli Escherichia coli - genetics Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Genetic Complementation Test Lysine - chemistry Lysine - metabolism Membrane Transport Proteins Molecular and cellular biology Molecular Sequence Data mutants Mutation Protein Precursors - metabolism SEC Translocation Channels SecA protein SecA Proteins Secretion. Exocytosis sites Temperature
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