FATRP_MYCTO
ID FATRP_MYCTO Reviewed; 631 AA.
AC P9WQJ2; L0T955; P63397; Q11047;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=MT1310;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45570.1; -; Genomic_DNA.
DR PIR; H70754; H70754.
DR RefSeq; WP_003406569.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQJ2; -.
DR SMR; P9WQJ2; -.
DR EnsemblBacteria; AAK45570; AAK45570; MT1310.
DR KEGG; mtc:MT1310; -.
DR PATRIC; fig|83331.31.peg.1415; -.
DR HOGENOM; CLU_000604_84_4_11; -.
DR Proteomes; UP000001020; 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_0000426766"
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