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3.A.1.122.18
MacAB-TolC MDR effllux porter. Exports macrolide antibiotics, virulence factors, peptides and cell envelope precursors. The 3-d crystal structure of MacB has been solved at 3.4 Å resolution (Okada et al. 2017). MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four TMSs that protrude in the periplasm into a binding domain for interaction with the membrane fusion protein MacA. It has unique structural features (Okada et al. 2017).

Accession Number:N9J6M5
Protein Name:Macrolide export ATP-binding/permease protein MacB
Length:664
Molecular Weight:71249.00
Species:Acinetobacter baumannii NIPH 601 [1217637]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTKQALLEVS NLVREFPAGE STIQILKGID LTIYEGELVA IVGQSGSGKS TLMNILGCLD 
61:	RPTSGSYKVN GQETGKLEPD QLAQLRREYF GFIFQRYHLL GDLSAEGNVE VPAVYAGVTP 
121:	ADRKQRATAL LTELGLGTKT QNRPSQLSGG QQQRVSIARA LMNGGDVILA DEPTGALDSH 
181:	SGVEVMRILR ELNAAGHTII LVTHDMQVAK NATRIIEISD GEIISDRPNV PDQSLEEVKS 
241:	DPDAAPALQN KQKKGKSISA WRSTLDRLSE AFQMALLSMN AHRMRTFLTM LGIIIGIASV 
301:	VTVVALGNGS QQQILSNISS LGTNTITVFQ GRGFGDNSKT ANFKTLVPAD ADALMTQPYV 
361:	SAVSPMVSTS KTMRYQQNEA NATINGVSND YFDVKGLVFK DGQTFDQRSV RDRSQDVVID 
421:	TNTQKQFFSD GTNPIGQVVL LGSVPARIIG IVEPQTSGMG SDDTLNVYMP YTTVMSRMLG 
481:	QAHVRNIVVR INDKYSTSAA ENAIVNLLTQ RHGAQDIFTM NSDSIRQTIE KTTSTMTLLV 
541:	SAIAVISLVV GGIGVMNIML VSVTERTQEI GVRMAVGARQ SDILQQFLIE AILVCLIGGV 
601:	LGVLLSLGLG QLINKFAGGN FAVAYSTTSI VAAFVCSTLI GVVFGFLPAK NAAKLDPVAA 
661:	LSRE