MACB_BRUA2
ID MACB_BRUA2 Reviewed; 646 AA.
AC Q2YRG7; Q2YRG8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=BAB1_1683/BAB1_1684;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ11639.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC Sequence=CAJ11640.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; AM040264; CAJ11639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AM040264; CAJ11640.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2YRG7; -.
DR SMR; Q2YRG7; -.
DR STRING; 359391.BAB1_1684; -.
DR EnsemblBacteria; CAJ11639; CAJ11639; BAB1_1683.
DR EnsemblBacteria; CAJ11640; CAJ11640; BAB1_1684.
DR KEGG; bmf:BAB1_1683; -.
DR KEGG; bmf:BAB1_1684; -.
DR HOGENOM; CLU_000604_8_5_5; -.
DR Proteomes; UP000002719; Chromosome I.
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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269926"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 7..245
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 646 AA; 68958 MW; 4A24AFC6B5D1568A CRC64;
MAGAPLIRLE DICKTFHNGD LAVEVLHGIT LDIRAGEFVA IMGASGSGKS TLMNILGCLD
TPTGGRYLLD GEDVSTLNAD ELATLRRRTF GFVFQSYNLI PTSTAQENVE VPAIYAGTPA
AERRKRAAAL LNALKLGDRL DHRPSQLSGG QQQRISIARA LMNGGRIILA DEPTGALDSQ
SGEDVMELLR SMHQQGHTVI VITHAREVAE RADRLIEIRD GQILSDTTKR DIHTPEATLQ
PHEEIAGNGA HIADISEAVK MALHALRANI FRTVLTLLGI IIGVSSVVTM LAIGTGAQNT
ILDRINAMGT DLILVRPAMA GFRGSGSIAT LVPQDADAIL ELPNVKSAVP EVTGTVTLRR
GNVDYQSQAN GTVPAFSSEI VESRQRQLHH PERYRYLRPC GWLGTTVVKT LFPDGGNPVG
DYILIQKIPF QIIGTLEPKG AGFGGSDQDD VVVVPLSTGN LRLFGQKYVR SITVQVKDSS
LIDTTQNQIQ SLLDQRHKKR DTMITNMSSV REDAAAMGKT MTVFLGSVAA ISLLVGGIGV
MNIMLVSVTE RTREIGVRMA TGARRRDILL QFIIEALSVS AIGGAIGVIL GLGAAALASW
AGLSVGYSFG PVLLAFACAF ATGLIFGFLP ARKASRLLPA VALSSE
