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. 2023 Jan 4;13:1042505. doi: 10.3389/fmicb.2022.1042505

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Copyright © 2023 Robinson, Collins, Murphy, Davies and Allsopp.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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In silico analysis of the vgrG7 island shows that it contains a putative lipase effector. (A) Comparative visualisation of the vgrG7 island in reference P. aeruginosa strains PAK and PA7 (CP000744.1). (B) Partial amino acid sequence alignment of PAKAF_03765 (Tle2^PAK) from PAK to Tle2^VC (TseL/VC_1418, AAF94575.1) from Vibrio cholerae O1 biovar El Tor str. N16961. The catalytic residues are indicated by a # and highlighted yellow. The GxSxG motif is highlighted in red. An asterisk (*) indicates fully conserved residues, a colon (:) indicates a strongly similar property at the residue, and a period (.) indicates a weakly similar property at the residue. The alignment was created using ClustalOmega (EMBL-EBI; Madeira et al., 2022). (C) Phyre2 predicted models of (i) DUF4123-containing protein (PAKAF_03768), (ii) VgrG7 (PAKAF_03769), (iii) Tli2_b (PAKAF_03767), (iv) Tli2_a (PAKAF_03766), and (v) Tle2 (PAKAF_03765).