Cloning, sequencing, and characterization of the secE homolog from coryneform bacteria.
Recent Res. Devel. 2: 429-435. 1998.
M. Kobayashi, Y. Asai and H. Yukawa.

A conserved domain of the secE gene from Bacillus subtilis and Escherichia coliwas used to desigh degenerate olirodeoxynucleotides. These synthetic DNA sequences were used to screen a lambda library of Brevibacterium flavum MJ233. A 1.4 kb PstI fragment of a recombinant lambda phage contaning the secE homolog from Br. flavum MJ233 was subsequentry subcloned into plasmid pUC118. The complete nucleotide sequence (nt) of the cloned fragment indicated that the deduced gene product of the Br. flavum secE homolog is composed of 111 amino acid (aa) with a deduced molecular weight (MW) of 11,514. Comparison of this aa sequence to the corresponding sequences from E. coli, B. subtilis, and Staphylococcus carnosus revealed a high degree of conservation, and suggested that the Br. flavum secE homolog is a membrane protein containing one transmembrane segment. The Br. flavum SecE geneproduct could replace the E. coli SecE protein in secE mutants.