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2.A.6.2.40
MDR pump, AdeABC (Acinetobacter drug efflux B = AdeB).It exports chloramphenicol and tetracycline (Hassan et al., 2011), but also confers resistance to meropenem, tigecycline and ceftazidime (Peleg et al. 2007; Provasi Cardoso et al. 2016). Morgan et al. 2021 reported six structures of the trimeric AdeB multidrug efflux pump in the presence of ethidium bromide using single-particle cryo-EM. These structures allowed them to directly observe various novel conformational states of the AdeB trimer. The transmembrane region of trimeric AdeB can associate with formation of a trimeric assembly or dissociated into "dimer plus monomer" and "monomer plus monomer plus monomer" configurations. A single AdeB protomer can simultaneously anchor a number of ethidium ligands, and different AdeB protomers can bind ethidium molecules simultaneously. A drug transport mechanism was proposed that involves multiple multidrug-binding sites and various transient states of the AdeB membrane protein. This suggests that each AdeB protomer within the trimer binds and exports drugs independently (Morgan et al. 2021).

Accession Number:Q2FD70
Protein Name:AdeB, RND
Length:1036
Molecular Weight:112624.00
Species:Acinetobacter baumannii [470]
Number of TMSs:12
Substrate chloramphenicol, tetracycline, tigecycline, ceftazidime, meropenem, ethidium

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Structure:
6OWS     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MMSQFFIRRP VFAWVIAIFI IIFGLLSIPK LPIARFPSVA PPQVNISATY PGATAKTIND 
61:	SVVTLIEREL SGVKNLLYYS ATTDTSGTAE ITATFKPGTD VEMAQVDVQN KIKAVEARLP 
121:	QVVRQQGLQV EASSSGFLML VGINSPNNQY SEVDLSDYLV RNVVEELKRV EGVGKVQSFG 
181:	AEKAMRIWVD PNKLVSYGLS ISDVNNAIRE NNVEIAPGRL GDLPAEKGQL ITIPLSAQGQ 
241:	LSSLEQFKNI SLKSKTNGSV IKLSDVANVE IGSQAYNFAI LENGKPATAA AIQLSPGANA 
301:	VKTAEGVRAK IEELKLNLPE GMEFSIPYDT APFVKISIEK VIHTLLEAMV LVFIVMYLFL 
361:	HNVRYTLIPA IVAPIALLGT FTVMLLAGFS INVLTMFGMV LAIGIIVDDA IVVVENVERI 
421:	MATEGLSPKD ATSKAMKEIT SPIIGITLVL AAVFLPMAFA SGSVGVIYKQ FTLTMSVSIL 
481:	FSALLALILT PALCATILKP IDGHHQKKGF FAWFDRSFDK VTKKYELMLL KIIKHTVPMM 
541:	VIFLVITGIT FAGMKYWPTA FMPEEDQGWF MTSFQLPSDA TAERTRNVVN QFENNLKDNP 
601:	DVKSNTAILG WGFSGAGQNV AVAFTTLKDF KERTSSASKM TSDVNSSMAN STEGETMAVL 
661:	PPAIDELGTF SGFSLRLQDR ANLGMPALLA AQDELMAMAA KNKKFYMVWN EGLPQGDNIS 
721:	LKIDREKLSA LGVKFSDVSD IISTSMGSMY INDFPNQGRM QQVIVQVEAK SRMQLKDILN 
781:	LKVMGSSGQL VSLSEVVTPQ WNKAPQQYNR YNGRPSLSIA GIPNFDTSSG EAMREMEQLI 
841:	AKLPKGIGYE WTGISLQEKQ SESQMAFLLG LSMLVVFLVL AALYESWAIP LSVMLVVPLG 
901:	IFGAIIAIMS RGLMNDVFFK IGLITIIGLS AKNAILIVEF AKMLKEEGMS LIEATVAAAK 
961:	LRLRPILMTS LAFTCGVIPL VIATGASSET QHALGTGVFG GMISATILAI FFVPVFFIFI 
1021:	LGAVEKLFSS KKKISS