SOTB_ECOLI
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 03-AUG-2022, entry version 157.
DE RecName: Full=Sugar efflux transporter;
GN Name=sotB; Synonyms=ydeA; OrderedLocusNames=b1528, JW1521;
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=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 (TC
CC 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; P31122; -.
DR PRIDE; P31122; -.
DR EnsemblBacteria; AAC74601; AAC74601; b1528.
DR EnsemblBacteria; BAA15210; BAA15210; BAA15210.
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; SAHFTAY; -.
DR PhylomeDB; P31122; -.
DR BioCyc; EcoCyc:YDEA-MON; -.
DR BioCyc; MetaCyc:YDEA-MON; -.
DR PRO; PR:P31122; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1250.20; -; 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 Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 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
