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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:Q2FD69
Protein Name:AdeC, OMF
Length:469
Molecular Weight:51536.00
Species:Acinetobacter baumannii [470]
Number of TMSs:1
Substrate chloramphenicol, tetracycline, tigecycline, ceftazidime, meropenem, ethidium

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MENTMSKSAI VSRGLILSTL SVTLVACVNM QAPQPAITSH IPQNFSQNHS GKTIAEKSYK 
61:	EFISDPKLVQ VIEISLNNNR DLRTATLNIE RVQQQYQITK NSQLPTIGVT GNAVRQVSPS 
121:	INPNNPVSTF QVGLGMTAYE LDFWGRVQNL KDAALNNYLA TQSAKEAVQI SLISNITQVW 
181:	LNYAFAQANL NLAEQTLKAQ VDAYNLNKKR FDVGIDSEVP LKQAQISVET ARNDVATYKT 
241:	QIQQAKNLLD LLAGHPVPQN LLPNHAIQNI TFEKNFAAGL PSDLLNHRPD LKAAEYELRA 
301:	AGANIGAAKA RMFPTISLTG STGYASSELK DLFKTGNFAW SIGPNIDLPI FDWGTRKTNI 
361:	KIAETDQKIA LAKYEKAIQS AFREVNDALA THAHIGERLD AQRRLVSATA ATYKLSMARY 
421:	RAGVDSYFTV LDAQRSAYAA QQGLLALEQM ELNNQIELYK VLGGGISKV