| Gelatinase biosynthesis activating pheromone | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | Enterococcus faecalis | ||||||
| Symbol | fsrD | ||||||
| UniProt | G8ADN7 | ||||||
| |||||||
Gelatinase biosynthesis-activating pheromone abbreviated as GBAP is a cyclic peptide produced by pathogenic bacteria such as Enterococcus faecalis. GAP is part of the quorum sensing system of certain bacteria where it positively regulates the expression of gelatinase and serine proteases that are under the control of the gelE-sprE operon.
GBAP is an 11-amino-acid-residue cyclic peptide containing a lactone linkage between the C-terminal carboxylic acid group and a serine side chain hydroxyl group.
References
- Teixeira N, Santos S, Marujo P, Yokohata R, Iyer VS, Nakayama J, Hancock LE, Serror P, Silva Lopes Mde F (2012). "The incongruent gelatinase genotype and phenotype in Enterococcus faecalis are due to shutting off the ability to respond to the gelatinase biosynthesis-activating pheromone (GBAP) quorum-sensing signal". Microbiology. 158 (Pt 2): 519–28. doi:10.1099/mic.0.055574-0. PMC 4083509. PMID 22117005.
- ^ Nishiguchi K, Nagata K, Tanokura M, Sonomoto K, Nakayama J (2009). "Structure-activity relationship of gelatinase biosynthesis-activating pheromone of Enterococcus faecalis". J. Bacteriol. 191 (2): 641–50. doi:10.1128/JB.01029-08. PMC 2620804. PMID 18996993.