ID   MACB_BURTA              Reviewed;         653 AA.
AC   Q2T4B3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=BTH_II1792;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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}.
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DR   EMBL; CP000085; ABC34957.1; -; Genomic_DNA.
DR   RefSeq; WP_009897901.1; NZ_CP008786.1.
DR   AlphaFoldDB; Q2T4B3; -.
DR   SMR; Q2T4B3; -.
DR   EnsemblBacteria; ABC34957; ABC34957; BTH_II1792.
DR   KEGG; bte:BTH_II1792; -.
DR   HOGENOM; CLU_000604_78_1_4; -.
DR   OMA; VVILITH; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000001930; Chromosome II.
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..653
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269932"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        587..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        616..636
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   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   653 AA;  70211 MW;  53B6790D004EDF9A CRC64;
     MAEPLLQLTR VTRRFPAGDK DVVVLDDVSL SIDAGEIVAI VGASGSGKST LMNILGCLDH
     PSSGSYRVGA RETSELESDE LARLRREHFG FIFQRYHLLP HLSAAENVEM PAVYAGSAQA
     QRRERALMLL ARLGLSDRAG HRPSQLSGGQ QQRVSIARAL MNGGEVILAD EPTGALDSKS
     GHDVIRVLRE LNALGHTVII VTHDENVAAH ARRIIEISDG RIVGDRLNPH ADGADAASGA
     SGDAGPQRAR RLSAGVGRFA EAFRMAWIAL VSHRLRTLLT MLGIIIGITS VVSIVAIGEG
     AKRYMLDEIG SIGTNTINVY PGADWGDSRA DAIQTLVPAD AAALADQIYV DSATPETSRS
     LLLRYRNIDV NALVSGVGER FFQVRGMKMA QGIAFGPDEV RRQAQVAVID ENTRRKLFGA
     NPNPLGEVIL IDNLPCIVIG VTAAKKSAFG DTKNLNVWVP YTTASGRLFG QRHLDSITVR
     VRDGQPSAAA EQSLTKLMLQ RHGRKDFFTY NMDSVVKTVE KTGQSLTLLL SLIAVISLVV
     GGIGVMNIML VSVTERTREI GIRMAVGARQ ADIMQQFLVE AVTVCLMGGA IGIVLSLGMS
     FVFSLFVDQW KMVFSAGSIV SAFLCSTLIG VVFGFMPARN ASRLDPIDAL ARD