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Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8
The authors have cloned the serine protease gene of Staphylococcus aureus , strain V8, as a 2.1 kilobase HindIII fragment in pBR322. The primary structure, deduced from the nucleotide sequence, contains two notable features not revealed by the directly determined partial amino acid sequence. First,...
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Published in: | Nucleic acids research 1987-08, Vol.15 (16), p.6757-6757 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | The authors have cloned the serine protease gene of Staphylococcus aureus , strain V8, as a 2.1 kilobase HindIII fragment in pBR322. The primary structure, deduced from the nucleotide sequence, contains two notable features not revealed by the directly determined partial amino acid sequence. First, the primary translation product contains a 68 residue NH2-terminal sequence not present in the secreted form of the protease. This extension, which begins with a signal peptide of 19-29 residues, is analogous to the prepro regions of the alkaline proteases of Bacillus species. Second, the COOH-terminal region, whose unusual amino acid composition is known, contains a twelvefold repeated tripeptide (residues 221-256) having proline in the first position, asparagine or aspartic acid in the second position, and, with a single exception, asparagine in the third position. |
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ISSN: | 0305-1048 1362-4962 |
DOI: | 10.1093/nar/15.16.6757 |