Abstract
A DNA fragment that codes for the 364 amino-terminal amino acid residues of a putative Bacillus subtilis SecA homologue has been cloned using the Escherichia coli secA gene as a probe. The deduced amino acid sequence showed 58% identity to the amino-terminus of the E. coli SecA protein. A DNA fragment which codes for 275 amino-terminal amino acid residues of the B. subtilis SecA homologue was expressed in E. coli and the corresponding gene product was shown to be recognized by anti-E. coli SecA antibodies. This polypeptide, although only about 30% the size of the E. coli SecA protein, also restored growth of E. coli MM52 (secAts) at the non-permissive temperature and the translocation defect of proOmpA in this mutant was relieved to a substantial extent.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / genetics*
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Amino Acid Sequence
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Autoradiography
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Bacillus subtilis / genetics*
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism*
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Base Sequence
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Biological Transport
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DNA, Bacterial / genetics
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics
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Escherichia coli Proteins*
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Genes, Bacterial*
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Gram-Negative Bacteria / metabolism*
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Gram-Positive Bacteria / metabolism*
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Membrane Transport Proteins*
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Molecular Sequence Data
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Restriction Mapping
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SEC Translocation Channels
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SecA Proteins
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Sequence Alignment
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Sequence Homology, Nucleic Acid
Substances
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Bacterial Proteins
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DNA, Bacterial
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Escherichia coli Proteins
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Membrane Transport Proteins
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SEC Translocation Channels
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Adenosine Triphosphatases
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SecA Proteins