Premium
The Pseudomonas aeruginosa patatin‐like protein PlpD is the archetype of a novel Type V secretion system
Author(s) -
Salacha Richard,
Kovačić Filip,
BrochierArmanet Céline,
Wilhelm Susanne,
Tommassen Jan,
Filloux Alain,
Voulhoux Romé,
Bleves Sophie
Publication year - 2010
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/j.1462-2920.2010.02174.x
Subject(s) - biology , secretion , signal peptide , bacterial outer membrane , bacteria , secretory protein , pseudomonas aeruginosa , biochemistry , transporter , peptide sequence , microbiology and biotechnology , gene , genetics , escherichia coli
Summary 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.