ID   MACB_BURCA              Reviewed;         681 AA.
AC   Q1BPZ6; Q1BPZ7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
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};
GN   OrderedLocusNames=Bcen_3413/Bcen_3414;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Non-canonical ABC transporter that contains transmembrane
CC       domains (TMD), which form a pore in the inner membrane, and an ATP-
CC       binding domain (NBD), which is responsible for energy generation.
CC       Confers resistance against macrolides. {ECO:0000255|HAMAP-
CC       Rule:MF_01720}.
CC   -!- SUBUNIT: Homodimer. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF78308.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC       Sequence=ABF78309.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR   EMBL; CP000379; ABF78308.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP000379; ABF78309.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q1BPZ6; -.
DR   SMR; Q1BPZ6; -.
DR   EnsemblBacteria; ABF78308; ABF78308; Bcen_3413.
DR   EnsemblBacteria; ABF78309; ABF78309; Bcen_3414.
DR   KEGG; bcn:Bcen_3413; -.
DR   KEGG; bcn:Bcen_3414; -.
DR   HOGENOM; CLU_000604_8_0_4; -.
DR   OMA; EGREHHK; -.
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; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..681
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269928"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        611..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        644..664
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          246..298
FT                   /note="Disordered"
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   681 AA;  72597 MW;  C20D196EC667FF65 CRC64;
     MRQPLLKLAA VTRRFPAGDK DVVVLNNVNL SIGAGEIVAI VGASGSGKST LMNILGCLDH
     PSEGTYTVGG RDTHMLDSDE LAQLRREHFG FVFQRYHLLP HVDAVANLEM PAIYAGTPRA
     DRHARARELL ARLGLADRAH HRPGQLSGGQ QQRVSIARAL MNGGQVILAD EPTGALDTKS
     GQDVIRILHE LNALGHTIVI VTHDKAVARH ARRIIEISDG EIVADRPNRH YAEAFAEVGV
     GAAATTETAA DTRSAPASGD APPPANNDTA ADPAPAPDAS PPAPAVSPKH AGWRGSRSCR
     TGCARCLTML GIIIGITSVV SIVAVGEGAK RYMLEEIGSI GTNTISLYPG SDWGDSRADT
     IQTLVPADVA ALAEQPYVDS ATPETSRTLL LRYRNVDVHA LVSGVGDSYF QTRGMRFALG
     VPFDDDAVRR QAQVAVIDQN TRRKLFGATR NPVGEAILVD NVPCVVIGVT ADKKSAFGSV
     KSLNVWVPYT TASGRLFGQR YLDSITVRVR DGQPSAAAEK SLEKLMIQRH GRKDFFTYNM
     DSVVKTVEKT GQSLTLLLSL IAVISLVVGG IGVMNIMLVS VTERTREIGI RMAVGARQSD
     ILQQFLVEAV LVCLLGGTIG IALSFGLGAL FSVFVAQWKM VFSAGAIVTA FVCSTLTGVI
     FGFMPARNAS RLDPIDALAR D