Using the gene fusion methodology adapted to mycobacteria, several DNA fragments encoding exported proteins were recently identified. In this paper, the molecular cloning, genomic positioning, nucleotide sequence determination and transcriptional start site mapping of a new gene, identified by this methodology, are reported. This gene was called (for exported epetitive rotein) and has a sequence similar to that of the 28 kDa antigen gene gene contains a putative iron box close to the mapped transcriptional start site. The predicted Erp protein displays a typical N-terminal signal sequence, a hydrophobic domain at the C-terminus and harbours repeated amino acid motifs. These structural features are reminiscent of cell-wall-associated surface proteins from Gram-positive bacteria. We found that these repeats are conserved among isolates, and are absent from the published gene sequence. In addition to being present in sequences were found in other members of the complex, but not in other mycobacteria tested. These results suggest that might encode a cell surface component shared by major pathogenic mycobacteria.


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