ID   MACB_HAEDU              Reviewed;         696 AA.
AC   Q7VMF9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=HD_1019;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the tripartite efflux system MacAB-TolC. MacB is a
CC       non-canonical ABC transporter that contains transmembrane domains
CC       (TMD), which form a pore in the inner membrane, and an ATP-binding
CC       domain (NBD), which is responsible for energy generation. Confers
CC       resistance against macrolides. {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TolC,
CC       which is composed of an inner membrane transporter, MacB, a periplasmic
CC       membrane fusion protein, MacA, and an outer membrane component, TolC.
CC       The complex forms a large protein conduit and can translocate molecules
CC       across both the inner and outer membranes. Interacts with MacA.
CC       {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01720}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01720}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC       exporter (TC 3.A.1.122) family. {ECO:0000255|HAMAP-Rule:MF_01720}.
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DR   EMBL; AE017143; AAP95897.1; -; Genomic_DNA.
DR   RefSeq; WP_010944947.1; NC_002940.2.
DR   AlphaFoldDB; Q7VMF9; -.
DR   SMR; Q7VMF9; -.
DR   STRING; 233412.HD_1019; -.
DR   EnsemblBacteria; AAP95897; AAP95897; HD_1019.
DR   KEGG; hdu:HD_1019; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_1_6; -.
DR   OMA; VVILITH; -.
DR   Proteomes; UP000001022; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003838; ABC3_permease_dom.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR017911; MacB_ATP-bd.
DR   InterPro; IPR025857; MacB_PCD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF02687; FtsX; 1.
DR   Pfam; PF12704; MacB_PCD; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51267; MACB; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..696
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269943"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        626..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        659..679
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          6..244
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   REGION          254..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   696 AA;  77356 MW;  4EB557811484FC98 CRC64;
     MKQPLIELKN IERYHTNGDT LTTVLKSINL KIYSGEMVAI VGASGSGKST LMNIIGALDV
     PNSGEYFIYG RNIADLSGDE LAELRCRHFG FVFQRYHLLS HLTAVKNVEV PAIYAMADKI
     LRNQRANALL CQLGLEKQLE NKPAQLSGGQ QQRVSIARAL MNGGDIILAD EPTGALDSQS
     SQDVLKILKD LNRKGHTVIL ITHDLAIAEH ADRVICIQDG KIVSDTANAL ESMIKPQNKR
     TFIDDAVIEV CQQHNTEKLN RPNEKNNIDN DNKENNNGYN RNDNSFLNNP KKKLNSSILR
     SFNSYAESFF MAFNMMMAHK IRTFLTMLGI IIGIIAVVFV IALGEGTKKK VLDEFSSLGN
     NTIDIFPGKW GDESDNVHTL NMEDLELLYQ QPYVQRATPV LLHIAKARYL NKTMRSLING
     VSHDFFMLKN YQLVTGRLFD QNDLTLSQPV GVIDKKSAKL LFDMDDPINK IIFIDDIPLS
     IIGVVESSSL QQNSGKEILI WIPHSTMATR ILNQSYIQQI SVQLQPNVSP LKSDKAIIDL
     LTIKHGQKDF YTFSSSRFLQ SLNKTTQALT LMISSIAFIS LIVGGIGIMN IMLVSVIERT
     KEIGIRIAVG AKERDIRFQF LIESTMVSLI GGCIGVGCAL LFGGLFSLAE TSIKIQFTLS
     SFLIAFLCSS MIGIVFGYFP ARNAAKLRPV DALSRE