Subunit
Homotrimer, with large porter and funnel domains (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:19023693, PubMed:28355133, PubMed:31201302). Extends into the periplasm, where the trimer interacts with AcrA and TolC (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:19023693, PubMed:28355133, PubMed:31201302). Component of the AcrAB-TolC multidrug efflux complex, composed of six AcrA subunits forming a hexameric tube, binding to an AcrB trimer, which interact with the trimeric TolC outer membrane channel protein (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:24747401, PubMed:28355133, PubMed:31201302). TolC is thought to not contact AcrB stably; instead, AcrA joins AcrB and TolC by forming a funnel-like hexamer anchored to the inner membrane (PubMed:15228545, PubMed:24747401, PubMed:28355133, PubMed:31201302). AcrA may initially form a hexameric ring complex with AcrB, in a bipartite complex, which may be stabilized by binding of AcrA with the peptidoglycan layer, prior to forming the full AcrAB-TolC efflux pump complex (PubMed:22308040, PubMed:28355133, PubMed:31201302). Contact between AcrA-AcrB and TolC may prompt a conformational change in the presence of substrate, allowing the periplasmic gate to open (PubMed:28355133, PubMed:31201302). Each AcrB protomer adopts one of three different conformational states, probably cycling between access, binding, and extrusion of substrate (PubMed:10920254, PubMed:12374972, PubMed:12738864, PubMed:15228545, PubMed:16079137, PubMed:16915237, PubMed:16946072, PubMed:17015667, PubMed:17194213, PubMed:19023693, PubMed:19425588, PubMed:25248080, PubMed:28355133, PubMed:31201302). Several charged residues in the transmembrane region of AcrB may constitute a proton translocation pathway, playing a key energetic role in the conformational changes driving efflux (PubMed:17015667, PubMed:19425588, PubMed:25248080). It is thought that, under high intracellular substrate concentration, AcrB ejects substrate into the tunnel formed by AcrA-TolC; as the substrate level declines, conformational changes in AcrB cause efflux to reduce and stop and the whole complex shifts to the closed state (PubMed:16915237, PubMed:16946072, PubMed:17194213, PubMed:25248080, PubMed:28355133, PubMed:31201302). Interacts with AcrZ; the interaction is direct (PubMed:23010927, PubMed:32348749). Component of the AcrABZ-TolC efflux pump complex, composed of six AcrA subunits forming a hexameric tube binding to an AcrB trimer, which interact with the trimeric TolC outer membrane channel protein; AcrZ interacts directly with AcrB, probably in 1:1 stoichiometry (PubMed:23010927, PubMed:24747401, PubMed:28355133, PubMed:32348749)