ID   BFE_SHEON               Reviewed;         452 AA.
AC   Q8EIX5;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=FAD transporter {ECO:0000303|PubMed:23322638};
DE   AltName: Full=Bacterial flavin adenine dinucleotide exporter {ECO:0000303|PubMed:23322638};
DE            Short=Bacterial FAD exporter {ECO:0000303|PubMed:23322638};
GN   Name=bfe {ECO:0000303|PubMed:23322638};
GN   OrderedLocusNames=SO_0702 {ECO:0000312|EMBL:AAN53780.1};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MR-1;
RX   PubMed=23322638; DOI=10.1128/mbio.00553-12;
RA   Kotloski N.J., Gralnick J.A.;
RT   "Flavin electron shuttles dominate extracellular electron transfer by
RT   Shewanella oneidensis.";
RL   MBio 4:E00553-E00553(2013).
CC   -!- FUNCTION: Flavin adenine dinucleotide (FAD) transporter that
CC       facilitates export of flavin electron shuttles.
CC       {ECO:0000269|PubMed:23322638}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:23322638}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene results in a severe decrease
CC       in flavin export. Mutants lacking the gene have no defect in reduction
CC       of soluble Fe(III), but they are deficient in the rate of insoluble
CC       Fe(III) oxide reduction. {ECO:0000269|PubMed:23322638}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC       2.A.66.1) family. {ECO:0000305}.
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DR   EMBL; AE014299; AAN53780.1; -; Genomic_DNA.
DR   RefSeq; NP_716335.1; NC_004347.2.
DR   RefSeq; WP_011071020.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EIX5; -.
DR   SMR; Q8EIX5; -.
DR   STRING; 211586.SO_0702; -.
DR   PaxDb; Q8EIX5; -.
DR   DNASU; 1168562; -.
DR   KEGG; son:SO_0702; -.
DR   PATRIC; fig|211586.12.peg.677; -.
DR   eggNOG; COG0534; Bacteria.
DR   HOGENOM; CLU_012893_5_3_6; -.
DR   OMA; VGNWIGS; -.
DR   OrthoDB; 216729at2; -.
DR   PhylomeDB; Q8EIX5; -.
DR   BioCyc; SONE211586:G1GMP-662-MON; -.
DR   Proteomes; UP000008186; 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:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR002528; MATE_fam.
DR   Pfam; PF01554; MatE; 2.
DR   PIRSF; PIRSF006603; DinF; 1.
DR   TIGRFAMs; TIGR00797; matE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..452
FT                   /note="FAD transporter"
FT                   /id="PRO_0000447490"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  48535 MW;  98050B1CEE72EC59 CRC64;
     MKDRHGLLSA PIGRVLLNMS LPNLIGIMTI LGFSLADTFF ISQLGTEALA AISFTFPVTL
     IISSIAIGVG AGVSTNLGRL IGSGNAPQAK VFLHDALLLT FILIASLSAL GSIFIEPLFS
     LLGANETSLP LIHDYMMYWY VGAPLLVLLM VGNQGLRSTG DTRSPAMIMT LAAIINLILD
     PLLIFGIGPF PRLEIQGAAI ATLFSWLVAL SLSGYLLIIK HRMLERAAFD IDRMRANWSK
     LAHIAQPAAL MNLINPLANA VIMAMLAHID HSAVAAFGAG TRLESVLLIV VMALSSSLMP
     FIAQNLGAGQ PQRAKQALLL SLKFILVFQT LLYIPLAFFA QPLASLFSTD PQVLEWLSFY
     ILVLPCAYGP LGIVIIFATA LNAYHRPMSS LVINLCRLVL LMLPLAALGS YIDGVKGLLL
     ALPITNLLMG IACYYLAQRI CEPVKATTAD TL