Cloning and expression of the gene for a protein disulfide oxidoreductase from Azotobacter vinelandii: complementation of an Escherichia coli dsbA mutant strain.

Abstract excerpt

The gene for a disulfide oxidoreductase was cloned and sequenced from Azotobacter vinelandii and termed the dsbA locus. The deduced amino acid sequence contains 214 residues with a potential 17-residue signaling sequence on the N-terminal end. This gives the mature protein a calculated molecular mass of 21 799 Da. The A. vinelandii DsbA protein contains the well-conserved motif of C-P-H-C, which is found in the...

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