TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


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:Q2FD71
Protein Name:AdeA, membrane fusion protein
Length:399
Molecular Weight:43705.00
Species:Acinetobacter baumannii [470]
Substrate chloramphenicol, tetracycline, tigecycline, ceftazidime, meropenem, ethidium

Cross database links:

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MDSMQKHLLL PLFLSIGLIL QGCDSKEVAQ AEPPPAKVSV LSIQPQSVNF SENLPARVHA 
61:	FRTAEIRPQV GGIIEKVLFK QGSEVRAGQA LYKINSETFE ADVNSNRASL NKAEAEVARL 
121:	KVQLERYEQL LPSNAVSKQE VSNAQAQYRQ ALADVAQMKA LLARQNLNLQ YATVRAPISG 
181:	RIGQSFVTEG ALVGQGDTNT MATIQQIDKV YVDVKQSVSE YERLQAALQS GELSANSDKT 
241:	VRITNSHGQP YNVTAKMLFE DINVDPETGD VTFRIEVNNT ERKLLPGMYV RVNIDRASIP 
301:	QALLVPAQAI QRNISGEPQV YVINAQGTAE IRPIEIGHQY EQFYIANKGL KVGDKVVVEG 
361:	IERIKPNQKL ALAVWKAPAV ANHASSVETK TSIAEGAQP