ID   MACB_BURP1              Reviewed;         653 AA.
AC   Q3JGG7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-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=BURPS1710b_A2185;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000125; ABA53400.1; -; Genomic_DNA.
DR   RefSeq; WP_004523215.1; NC_007435.1.
DR   AlphaFoldDB; Q3JGG7; -.
DR   SMR; Q3JGG7; -.
DR   EnsemblBacteria; ABA53400; ABA53400; BURPS1710b_A2185.
DR   KEGG; bpm:BURPS1710b_A2185; -.
DR   HOGENOM; CLU_000604_78_2_4; -.
DR   OMA; VVILITH; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000002700; 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_0000269930"
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;  70312 MW;  EC9A3DEC22D9210A CRC64;
     MTGPLLQLTR VTRRFPAGEK DVVVLDDVSL SIDAGEIVAI VGASGSGKST LMNILGCLDH
     PSSGSYTVGG RETSELESDE LARLRREHFG FIFQRYHLLP HLCAAENVEM PAVYAGSAQA
     QRRERALALL ARLGLSDRAS HRPSQLSGGQ QQRVSIARAL MNGGEVILAD EPTGALDSKS
     GRDVIRVLRE LNALGHTVII VTHDEQVAAH ARRIIEISDG RIVGDRLNPH ADAADAAPDA
     SGGAQPQRAR RLSAGVGRFA EAFRMAWIAL VSHRLRTLLT MLGIIIGITS VVSIVAIGEG
     AKRYMLDEIG SIGTNTINVY PGADWGDSRA DAIQTLVAAD AAALADQIYI DSATPETSRS
     LLLRYRNVDV NALVSGVGER FFQVRGMKLA QGIAFGADEV RRQAQVAVID ENTRRKLFGA
     NPNPLGEVIL IDNLPCVVIG VTASKKSAFG DMKNLNVWVP YTTASGRLFG QRHLDSITVR
     VRDGQPSDAA ERSLTKLMLQ RHGRKDFFTY NMDSVVKTVE KTGQSLTLLL SLIAVISLVV
     GGIGVMNIML VSVTERTREI GIRMAVGARQ TDIMQQFLVE AVTVCLMGGA IGIVLSFGMS
     FVFSLFVDQW KMVFSAASIA SAFLCSTLIG VVFGFMPARN ASRLDPIDAL ARD