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The Pseudomonas aeruginosa patatin-like protein PlpD is the archetype of a novel Type V secretion system

Abstract : P>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 beta-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.
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https://hal.archives-ouvertes.fr/hal-00698204
Contributor : Stéphane Delmotte Connect in order to contact the contributor
Submitted on : Wednesday, May 16, 2012 - 2:06:31 PM
Last modification on : Monday, April 25, 2022 - 5:45:22 PM

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R. Salacha, F. Kovacic, Céline Brochier-Armanet, S. Wilhelm, J. Tommassen, et al.. The Pseudomonas aeruginosa patatin-like protein PlpD is the archetype of a novel Type V secretion system. Environmental Microbiology, Society for Applied Microbiology and Wiley-Blackwell, 2010, 12 (6), pp.1498-512. ⟨10.1111/j.1462-2920.2010.02174.x⟩. ⟨hal-00698204⟩

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