YEEO_ECOLI
ID YEEO_ECOLI Reviewed; 547 AA.
AC P76352; P94752;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable FMN/FAD exporter YeeO;
GN Name=yeeO; OrderedLocusNames=b1985, JW1965;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN DIPEPTIDE EXPORT.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=20067529; DOI=10.1111/j.1574-6968.2009.01879.x;
RA Hayashi M., Tabata K., Yagasaki M., Yonetani Y.;
RT "Effect of multidrug-efflux transporter genes on dipeptide resistance and
RT overproduction in Escherichia coli.";
RL FEMS Microbiol. Lett. 304:12-19(2010).
RN [5]
RP FUNCTION IN FLAVIN EXPORT.
RC STRAIN=K12 / BW25113;
RX PubMed=25482085; DOI=10.4161/21655979.2014.969173;
RA McAnulty M.J., Wood T.K.;
RT "YeeO from Escherichia coli exports flavins.";
RL Bioengineered 5:386-392(2014).
CC -!- FUNCTION: A transporter able to export peptides and flavins. When
CC overexpressed allows cells deleted for multiple peptidases (pepA, pepB,
CC pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr
CC which otherwise inhibit growth (PubMed:20067529). Cells overexpressing
CC this protein have decreased intracellular levels of Ala-Gln dipeptide,
CC and in a system that produces the Ala-Gln dipeptide, overproduction of
CC this protein increases its export (PubMed:20067529). When overexpressed
CC increases secretion of FMN and FAD but not riboflavin; intracellular
CC concentrations of FMN and riboflavin rise, possibly to compensate for
CC increased secretion (PubMed:25482085). Increased overexpression causes
CC slight cell elongation (PubMed:25482085). {ECO:0000269|PubMed:20067529,
CC ECO:0000269|PubMed:25482085}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC75048.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC75048.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP009048; BAA15804.2; -; Genomic_DNA.
DR PIR; B64963; B64963.
DR RefSeq; NP_416491.2; NC_000913.3.
DR AlphaFoldDB; P76352; -.
DR SMR; P76352; -.
DR BioGRID; 4259355; 187.
DR STRING; 511145.b1985; -.
DR TCDB; 2.A.66.1.23; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; P76352; -.
DR PRIDE; P76352; -.
DR EnsemblBacteria; AAC75048; AAC75048; b1985.
DR EnsemblBacteria; BAA15804; BAA15804; BAA15804.
DR GeneID; 946506; -.
DR KEGG; ecj:JW1965; -.
DR KEGG; eco:b1985; -.
DR PATRIC; fig|511145.12.peg.2062; -.
DR EchoBASE; EB3164; -.
DR eggNOG; COG0534; Bacteria.
DR HOGENOM; CLU_012893_5_3_6; -.
DR InParanoid; P76352; -.
DR BioCyc; EcoCyc:YEEO-MON; -.
DR BioCyc; MetaCyc:YEEO-MON; -.
DR PRO; PR:P76352; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015230; F:FAD transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0044610; F:FMN transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IMP:EcoCyc.
DR GO; GO:0035350; P:FAD transmembrane transport; IDA:EcoCyc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR002528; MATE_fam.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; FMN; Membrane;
KW Peptide transport; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..547
FT /note="Probable FMN/FAD exporter YeeO"
FT /id="PRO_0000164253"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 547 AA; 60061 MW; 64239AEB52A0AC09 CRC64;
MLRHILTAKN LLSNPIFKFP NCLPFLSTVC CICRQFVGEN LCSFADSPSL FEMWFHFLQL
RSALNISSAL RQVVHGTRWH AKRKSYKVLF WREITPLAVP IFMENACVLL MGVLSTFLVS
WLGKDAMAGV GLADSFNMVI MAFFAAIDLG TTVVVAFSLG KRDRRRARVA TRQSLVIMTL
FAVLLATLIH HFGEQIIDFV AGDATTEVKA LALTYLELTV LSYPAAAITL IGSGALRGAG
NTKIPLLING SLNILNIIIS GILIYGLFSW PGLGFVGAGL GLTISRYIGA VAILWVLAIG
FNPALRISLK SYFKPLNFSI IWEVMGIGIP ASVESVLFTS GRLLTQMFVA GMGTSVIAGN
FIAFSIAALI NLPGSALGSA STIITGRRLG VGQIAQAEIQ LRHVFWLSTL GLTAIAWLTA
PFAGVMASFY TQDPQVKHVV VILIWLNALF MPIWSASWVL PAGFKGARDA RYAMWVSMLS
MWGCRVVVGY VLGIMLGWGV VGVWMGMFAD WAVRAVLFYW RMVTGRWLWK YPRPEPQKCE
KKPVVSE
