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MACB_BURL3
ID   MACB_BURL3              Reviewed;         687 AA.
AC   Q399M3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=Bcep18194_B0724;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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}.
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DR   EMBL; CP000152; ABB10838.1; -; Genomic_DNA.
DR   RefSeq; WP_011354332.1; NC_007511.1.
DR   AlphaFoldDB; Q399M3; -.
DR   SMR; Q399M3; -.
DR   EnsemblBacteria; ABB10838; ABB10838; Bcep18194_B0724.
DR   GeneID; 45097092; -.
DR   KEGG; bur:Bcep18194_B0724; -.
DR   PATRIC; fig|482957.22.peg.4342; -.
DR   HOGENOM; CLU_000604_78_1_4; -.
DR   OMA; VVILITH; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000002705; Chromosome 2.
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..687
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269931"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        617..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        650..670
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..281
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   687 AA;  74008 MW;  47BF6167D44D24E2 CRC64;
     MRQPLLKLAA VTRRFPAGDK DVVVLNNVNL SIHAGEIVAI VGASGSGKST LMNILGCLDH
     PSEGTYTVGG RDTHMLDSDE LAQLRREHFG FVFQRYHLLP HVDAVANLEM PAIYAGTPRA
     ERHARARELL ARLGLADRAH HRPGQLSGGQ QQRVSIARAL MNGGQVILAD EPTGALDTKS
     GQDVIRILHE LNALGHTIVI VTHDKAVARH AKRIIEISDG EIVADRPNRH YAEALAEAGV
     DAAEAAEASE AAVGESPTRN RHDTPAPPAA VDTDPHVDTG TRTRRFAAGS GRFAEACRMA
     WIALVSHRLR TLLTMLGIII GITSVVSIVA IGEGAKRYML DEIGSIGTNT INIYPGTDWG
     DSRADAIQTL VPADVAALTE QPYVDSATPE TSRTLLLRYR NVDVNALVSG VGDRFFQARG
     MRFALGVAFD EDAVRRQVQV AVIDQNTRRK LFGATRNPIG EVILVDNVPC VVIGVTADKK
     SAFGSVKSLN VWVPYTTASG RLFGQRYLDS ITVRVRDGQP SAAAEKSLEK LMTQRHGRKD
     FFTYNMDSVV KTVEKTGQSL TLLLSLIAVI SLVVGGIGVM NIMLVSVTER TREIGIRMAV
     GARQSDILQQ FLVEAVLVCL LGGTIGIALS FGLGALFSMF VAQWKMVFSA GAIVTAFVCS
     TLTGVIFGFM PARNASRLDP IDALARD
 
 
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