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).
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| Accession Number: | Q2FD52 |
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| Protein Name: | Efflux transporter, RND family, MFP subunit |
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| Length: | 445 |
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| Molecular Weight: | 48145.00 |
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| Species: | Acinetobacter baumannii [470] |
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| Number of TMSs: | 1 |
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| Substrate |
peptide, macrolide antibiotic, virulence factor |
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1: MPKIKPIKLV IIVVCIAIIA VLAWKFLKPK QQQPQYITAE VTRGDIENNV LATGTLDATK
61: LISVGAQVSG QVKKMYVQLG DQVKQGQLIA QIDSTTQENS LKTSDANIKN LEAQRLQQIA
121: SLNEKQLEYR RQQQMYAQDA TPRADLESAE AAYKTAQAQV KALDAQIESA KITRSTAQTN
181: IGYTRIVAPT DGTVVAIVTE EGQTVNANQS APTIVKIAKL QNMTIKAQVS EADIMKVEKG
241: QQVYFTTLGD ETKRYATLRQ IEPAPDSISS ESNSTTSSTT SSAVYYNALF DVPNTDGKLR
301: IDMTAQVYIV LNSAKNALLV PSSALSSKQF SGQRKQGQSA DKASSTPSAE RKHQGNGVRL
361: ERLNLTPEQK QLIEQGKATL SVVRVLQADG TTKPTQILVG INNRVNAQVL AGLKQGDQVV
421: IADSSENSAA SANSGNNRRR GPMGM