EFPA_MYCTU
ID EFPA_MYCTU Reviewed; 530 AA.
AC P9WJY5; L0TDQ9; O05813; Q50747; Q7D6G8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Uncharacterized MFS-type transporter EfpA;
DE AltName: Full=Efflux protein A;
GN Name=efpA; OrderedLocusNames=Rv2846c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9008277; DOI=10.1128/cdli.4.1.23-32.1997;
RA Doran J.L., Pang Y., Mdluli K.E., Moran A.J., Victor T.C., Stokes R.W.,
RA Mahenthiralingam E., Kreiswirth B.N., Butt J.L., Baron G.S., Treit J.D.,
RA Kerr V.J., Van Helden P.D., Roberts M.C., Nano F.E.;
RT "Mycobacterium tuberculosis efpA encodes an efflux protein of the QacA
RT transporter family.";
RL Clin. Diagn. Lab. Immunol. 4:23-32(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17590082; DOI=10.1371/journal.ppat.0030087;
RA Colangeli R., Helb D., Vilcheze C., Hazbon M.H., Lee C.G., Safi H.,
RA Sayers B., Sardone I., Jones M.B., Fleischmann R.D., Peterson S.N.,
RA Jacobs W.R. Jr., Alland D.;
RT "Transcriptional regulation of multi-drug tolerance and antibiotic-induced
RT responses by the histone-like protein Lsr2 in M. tuberculosis.";
RL PLoS Pathog. 3:E87-E87(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expressed during infection of macrophages. Down-regulated by
CC the nucleoid-associated protein Lsr2. {ECO:0000269|PubMed:17590082,
CC ECO:0000269|PubMed:9008277}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; L39922; AAA85344.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45647.1; -; Genomic_DNA.
DR PIR; A70589; A70589.
DR RefSeq; NP_217362.1; NC_000962.3.
DR RefSeq; WP_003414532.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P9WJY5; -.
DR SMR; P9WJY5; -.
DR STRING; 83332.Rv2846c; -.
DR DrugBank; DB05154; Pretomanid.
DR TCDB; 2.A.1.3.78; the major facilitator superfamily (mfs).
DR PaxDb; P9WJY5; -.
DR DNASU; 888575; -.
DR GeneID; 888575; -.
DR KEGG; mtu:Rv2846c; -.
DR TubercuList; Rv2846c; -.
DR eggNOG; COG0477; Bacteria.
DR OMA; GNKKGWL; -.
DR PhylomeDB; P9WJY5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="Uncharacterized MFS-type transporter EfpA"
FT /id="PRO_0000390888"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 50
FT /note="S -> T (in Ref. 1; AAA85344)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="A -> R (in Ref. 1; AAA85344)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..343
FT /note="AG -> R (in Ref. 1; AAA85344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 55580 MW; 189F752ECB053BED CRC64;
MTALNDTERA VRNWTAGRPH RPAPMRPPRS EETASERPSR YYPTWLPSRS FIAAVIAIGG
MQLLATMDST VAIVALPKIQ NELSLSDAGR SWVITAYVLT FGGLMLLGGR LGDTIGRKRT
FIVGVALFTI SSVLCAVAWD EATLVIARLS QGVGSAIASP TGLALVATTF PKGPARNAAT
AVFAAMTAIG SVMGLVVGGA LTEVSWRWAF LVNVPIGLVM IYLARTALRE TNKERMKLDA
TGAILATLAC TAAVFAFSIG PEKGWMSGIT IGSGLVALAA AVAFVIVERT AENPVVPFHL
FRDRNRLVTF SAILLAGGVM FSLTVCIGLY VQDILGYSAL RAGVGFIPFV IAMGIGLGVS
SQLVSRFSPR VLTIGGGYLL FGAMLYGSFF MHRGVPYFPN LVMPIVVGGI GIGMAVVPLT
LSAIAGVGFD QIGPVSAIAL MLQSLGGPLV LAVIQAVITS RTLYLGGTTG PVKFMNDVQL
AALDHAYTYG LLWVAGAAII VGGMALFIGY TPQQVAHAQE VKEAIDAGEL
