ID   FATRP_MYCBO             Reviewed;         631 AA.
AC   P63398; A0A1R3XXV7; Q11047; X2BHV5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Fatty acid ABC transporter ATP-binding/permease protein {ECO:0000250|UniProtKB:P9WQJ3};
DE            EC=7.6.2.- {ECO:0000250|UniProtKB:P9WQJ3};
GN   OrderedLocusNames=BQ2027_MB1303C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: ABC transporter involved in fatty acid import. Transmembrane
CC       domains (TMD) form a pore in the membrane and the ATP-binding domain
CC       (NBD) is responsible for energy generation.
CC       {ECO:0000250|UniProtKB:P9WQJ3}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P9WQJ3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DOMAIN: The ATP-binding domain (NBD) and the transmembrane domain (TMD)
CC       are fused. {ECO:0000250|UniProtKB:P9WQJ3}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid exporter
CC       (TC 3.A.1.106) family. {ECO:0000305}.
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DR   EMBL; LT708304; SIT99906.1; -; Genomic_DNA.
DR   RefSeq; NP_854957.1; NC_002945.3.
DR   RefSeq; WP_003406569.1; NC_002945.4.
DR   AlphaFoldDB; P63398; -.
DR   SMR; P63398; -.
DR   EnsemblBacteria; SIT99906; SIT99906; BQ2027_MB1303C.
DR   PATRIC; fig|233413.5.peg.1428; -.
DR   OMA; WGTYLVK; -.
DR   Proteomes; UP000001419; Chromosome.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..631
FT                   /note="Fatty acid ABC transporter ATP-binding/permease
FT                   protein"
FT                   /id="PRO_0000093262"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..365
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          397..631
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         430..437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   631 AA;  68305 MW;  7B7A2D5E91AD06ED CRC64;
     MTAPPGARPR AASPPPNMRS RDFWGSAARL VKRLAPQRRL SIAVITLGIA GTTIGVIVPR
     ILGHATDLLF NGVIGRGLPG GITKAQAVAS ARARGDNTFA DLLSGMNVVP GQGVDFAAVE
     RTLALALALY LAAALMIWAQ ARLLNLTVQK TMVRLRTDVE DKVHRLPLSY FDGQQRGELL
     SRVTNDIDNL QSSLSMTISQ LVTSILTMVA VLAMMVSISG LLALITLLTV PLSLLVTRAI
     TRRSQPLFVA HWTSTGRLNA HLEETYSGFT VVKTFGHQAA ARERFHELND DVYQAGFGAQ
     FLSGLVQPAT AFIGNLGYVA VAVAGGLQVA TGQITLGSIQ AFIQYIRQFN MPLSQLAGMY
     NALQSGVASA ERVFDVLDEP EESPEPEPEL PNLTGRVEFE HVNFAYLPGT PVIRDLSLVA
     EPGSTVAIVG PTGAGKTTLV NLLMRFYEIG SGRILIDGVD IASVSRQSLR SRIGMVLQDT
     WLYDGTIAEN IAYGRPEATT DEIVEAARAA HVDRFVNTLP AGYQTRVSGD GGSISVGEKQ
     LITIARAFLA RPQLLILDEA TSSVDTRTEL LIQRAMRELR RDRTSFIIAH RLSTIRDADH
     ILVVQTGQIV ERGNHAELLA RRGVYYQMTR A