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: | 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 |
peptide, macrolide antibiotic, virulence factor |
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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