ID   SOTB_ECOLI              Reviewed;         396 AA.
AC   P31122; P76883; P77353;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Sugar efflux transporter;
GN   Name=sotB; Synonyms=ydeA; OrderedLocusNames=b1528, JW1521;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; 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=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-396.
RX   PubMed=8383113; DOI=10.1128/jb.175.5.1484-1492.1993;
RA   Cohen S.P., Haechler H., Levy S.B.;
RT   "Genetic and functional analysis of the multiple antibiotic resistance
RT   (mar) locus in Escherichia coli.";
RL   J. Bacteriol. 175:1484-1492(1993).
RN   [5]
RP   CHARACTERIZATION.
RC   STRAIN=SB0;
RX   PubMed=10094697; DOI=10.1128/jb.181.7.2185-2191.1999;
RA   Bost S., Silva F., Belin D.;
RT   "Transcriptional activation of ydeA, which encodes a member of the major
RT   facilitator superfamily, interferes with arabinose accumulation and
RT   induction of the Escherichia coli arabinose PBAD promoter.";
RL   J. Bacteriol. 181:2185-2191(1999).
RN   [6]
RP   CHARACTERIZATION.
RC   STRAIN=JS219;
RX   PubMed=10438792; DOI=10.1128/jb.181.16.5123-5125.1999;
RA   Carole S., Pichoff S., Bouche J.-P.;
RT   "Escherichia coli gene ydeA encodes a major facilitator pump which exports
RT   L-arabinose and isopropyl-beta-D-thiogalactopyranoside.";
RL   J. Bacteriol. 181:5123-5125(1999).
RN   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
CC   -!- FUNCTION: Involved in the efflux of sugars. The physiological role may
CC       be the reduction of the intracellular concentration of toxic sugars or
CC       sugar metabolites. Transports L-arabinose and to a lesser extent IPTG.
CC       Seems to contribute to the control of the arabinose regulon.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. SotB
CC       (TC 2.A.1.2) family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74601.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15210.1; -; Genomic_DNA.
DR   EMBL; M96235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C64907; C64907.
DR   RefSeq; NP_416045.1; NC_000913.3.
DR   RefSeq; WP_000210799.1; NZ_SSZK01000001.1.
DR   PDB; 6KKI; X-ray; 3.06 A; A=1-396.
DR   PDB; 6KKJ; X-ray; 3.38 A; B=1-396.
DR   PDB; 6KKK; X-ray; 3.50 A; A/B/C=1-396.
DR   PDB; 6KKL; X-ray; 2.65 A; A=1-396.
DR   PDBsum; 6KKI; -.
DR   PDBsum; 6KKJ; -.
DR   PDBsum; 6KKK; -.
DR   PDBsum; 6KKL; -.
DR   AlphaFoldDB; P31122; -.
DR   SMR; P31122; -.
DR   BioGRID; 4259471; 243.
DR   STRING; 511145.b1528; -.
DR   TCDB; 2.A.1.2.15; the major facilitator superfamily (mfs).
DR   PaxDb; 511145-b1528; -.
DR   EnsemblBacteria; AAC74601; AAC74601; b1528.
DR   GeneID; 947218; -.
DR   KEGG; ecj:JW1521; -.
DR   KEGG; eco:b1528; -.
DR   PATRIC; fig|1411691.4.peg.738; -.
DR   EchoBASE; EB1592; -.
DR   eggNOG; COG2814; Bacteria.
DR   HOGENOM; CLU_001265_61_1_6; -.
DR   InParanoid; P31122; -.
DR   OMA; YTYLSPY; -.
DR   OrthoDB; 9788453at2; -.
DR   PhylomeDB; P31122; -.
DR   BioCyc; EcoCyc:YDEA-MONOMER; -.
DR   BioCyc; MetaCyc:YDEA-MONOMER; -.
DR   PRO; PR:P31122; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd17324; MFS_NepI_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   HAMAP; MF_00517; MFS_SotB; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR023495; Sugar_effux_transptr_put.
DR   PANTHER; PTHR43124; PURINE EFFLUX PUMP PBUE; 1.
DR   PANTHER; PTHR43124:SF4; SUGAR EFFLUX TRANSPORTER; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..396
FT                   /note="Sugar efflux transporter"
FT                   /id="PRO_0000209323"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..49
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..169
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..245
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        267..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..298
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..363
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   HELIX           10..30
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           31..34
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           36..43
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           47..50
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           52..71
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           77..96
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           101..128
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           136..151
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           153..164
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           166..187
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           201..206
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           209..229
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           232..238
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           244..294
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           298..326
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           331..359
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           362..364
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   HELIX           365..386
FT                   /evidence="ECO:0007829|PDB:6KKL"
FT   STRAND          389..391
FT                   /evidence="ECO:0007829|PDB:6KKK"
SQ   SEQUENCE   396 AA;  42538 MW;  CB6A34CA4EE6D4F0 CRC64;
     MTTNTVSRKV AWLRVVTLAV AAFIFNTTEF VPVGLLSDIA QSFHMQTAQV GIMLTIYAWV
     VALMSLPFML MTSQVERRKL LICLFVVFIA SHVLSFLSWS FTVLVISRIG VAFAHAIFWS
     ITASLAIRMA PAGKRAQALS LIATGTALAM VLGLPLGRIV GQYFGWRMTF FAIGIGALIT
     LLCLIKLLPL LPSEHSGSLK SLPLLFRRPA LMSIYLLTVV VVTAHYTAYS YIEPFVQNIA
     GFSANFATAL LLLLGGAGII GSVIFGKLGN QYASALVSTA IALLLVCLAL LLPAANSEIH
     LGVLSIFWGI AMMIIGLGMQ VKVLALAPDA TDVAMALFSG IFNIGIGAGA LVGNQVSLHW
     SMSMIGYVGA VPAFAALIWS IIIFRRWPVT LEEQTQ
//