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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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