| Literature DB >> 7512553 |
S Borchert1, T Stachelhaus, M A Marahiel.
Abstract
The deduced amino acid sequence of the gsp gene, located upstream of the 5' end of the gramicidin S operon (grs operon) in Bacillus brevis, showed a high degree of similarity to the sfp gene product, which is located downstream of the srfA operon in B. subtilis. The gsp gene complemented in trans a defect in the sfp gene (sfpO) and promoted production of the lipopeptide antibiotic surfactin. The functional homology of Gsp and Sfp and the sequence similarity of these two proteins to EntD suggest that the three proteins represent a new class of proteins involved in peptide secretion, in support of a hypothesis published previously (T. H. Grossman, M. Tuckman, S. Ellestad, and M. S. Osburne, J. Bacteriol. 175:6203-6211, 1993).Entities:
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Year: 1994 PMID: 7512553 PMCID: PMC205374 DOI: 10.1128/jb.176.8.2458-2462.1994
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490