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. 2015 Mar 12;6:170. doi: 10.3389/fmicb.2015.00170

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Copyright © 2015 Rojas Murcia, Lee, Waridel, Maspoli, Imker, Chai, Walsh and Reimmann.

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) or licensor 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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Organization of the amb gene cluster in the Pseudomonas aeruginosa strain PAO1. The ambA gene encodes a putative LysE-type transmembrane protein potentially involved in AMB export, ambB and ambE code for non-ribosomal peptide synthetases (NRPS), and ambC and ambD specify two putative iron (II)/α-ketoglutarate-dependent oxygenases. The modular structures of AmbB and AmbE are shown with domains for adenylation (A), thiolation (T), condensation (C), methylation (MT), and thioester cleavage (TE). Note that AmbE may have an additional domain of unknown function at its N-terminus and that the C domain (indicated as C*) is atypical (see text for details).