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. 2019 Jan 9;8(7):e00774. doi: 10.1002/mbo3.774

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© 2019 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.

This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Figure A4 — The T6SS‐7 cluster of B. cenocepacia H111 encodes a putative T6SS type‐5 lipase effector (Tle5) with characteristic dual HxKhhhhD sequence motifs.Amino acid sequence alignment of the two regions containing HxKhhhhD catalytic motifs present in putative T6SS‐dependent type‐5 lipase effector (Tle5) homologues from B. cenocepacia H111 (encoded within the T6SS‐7 cluster at I35_RS17370), B. cenocepacia J2315 (BCAM0149), R. solanacearum GMI1000 and CFBP2957 (RS_RS20135 and RCFBP_mp20221), C. violaceum ATCC 12472 (CV_RS06020), C. metallidurans CH42 (RMET_RS03180), P. aeruginosa PAO1 (PA5089 and PA3487), A. xylosoxidans A8 (AXYL_RS28255) and S. maltophilia SKK35 (SMSKK35_0837). The dual HxKhhhhD motif (where h is an amino acid with a hydrophobic side chain) is characteristic of phospholipase D (PLD) enzymes.