MACB_BURCH
ID MACB_BURCH Reviewed; 681 AA.
AC A0B212;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Bcen2424_4954;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-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}.
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DR EMBL; CP000459; ABK11688.1; -; Genomic_DNA.
DR RefSeq; WP_011694806.1; NC_008543.1.
DR AlphaFoldDB; A0B212; -.
DR SMR; A0B212; -.
DR KEGG; bch:Bcen2424_4954; -.
DR HOGENOM; CLU_000604_78_1_4; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
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_0000280163"
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..274
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; 72992 MW; 1D2F81729E4465DD 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 ADPAPRARRF AAGTGRFAEA CRMAWIALVS
HRLRTLLTML 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