The Pseudomonas aeruginosa patatin-like protein PlpD is the archetype of a novel Type V secretion system
Article first published online: 23 FEB 2010
© 2010 Society for Applied Microbiology and Blackwell Publishing Ltd
Special Issue: Pseudomonas. Editors: Professors Burkhard Tummler, Victor de Lorenzo, Alain Filloux and Joyce Loper
Volume 12, Issue 6, pages 1498–1512, June 2010
How to Cite
Salacha, R., Kovačić, F., Brochier-Armanet, C., Wilhelm, S., Tommassen, J., Filloux, A., Voulhoux, R. and Bleves, S. (2010), The Pseudomonas aeruginosa patatin-like protein PlpD is the archetype of a novel Type V secretion system. Environmental Microbiology, 12: 1498–1512. doi: 10.1111/j.1462-2920.2010.02174.x
- Issue published online: 3 JUN 2010
- Article first published online: 23 FEB 2010
- Received 12 November, 2009; accepted 22 December, 2009.
We discovered a novel secreted protein by Pseudomonas aeruginosa, PlpD, as a member of the bacterial lipolytic enzyme family of patatin-like proteins (PLPs). PlpD is synthesized as a single molecule consisting of a secreted domain fused to a transporter domain. The N-terminus of PlpD includes a classical signal peptide followed by the four PLP conserved blocks that account for its lipase activity. The C-terminus consists of a POTRA (polypeptide transport-associated) motif preceding a putative 16-stranded β-barrel similar to those of TpsB transporters of Type Vb secretion system. We showed that the C-terminus remains inserted into the outer membrane while the patatin moiety is secreted. The association between a TpsB component and a passenger protein is a unique hybrid organization that we propose to classify as Type Vd. More than 200 PlpD orthologues exist among pathogenic and environmental bacteria, which suggests that bacteria secrete numerous PLPs using this newly defined mechanism.