EXUT_ECOLI
ID EXUT_ECOLI Reviewed; 432 AA.
AC P0AA78; P42609; Q2M9B3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Hexuronate transporter {ECO:0000305};
DE AltName: Full=Aldohexuronate transport system {ECO:0000303|PubMed:783117};
DE Flags: Precursor;
GN Name=exuT {ECO:0000303|PubMed:783117}; OrderedLocusNames=b3093, JW3064;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Mizobuchi K.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=783117; DOI=10.1128/jb.127.2.706-718.1976;
RA Nemoz G., Robert-Baudouy J., Stoeber F.;
RT "Physiological and genetic regulation of the aldohexuronate transport
RT system in Escherichia coli.";
RL J. Bacteriol. 127:706-718(1976).
RN [5]
RP FUNCTION.
RX PubMed=6343797; DOI=10.1007/bf00337832;
RA Mata-Gilsinger M., Ritzenthaler P.;
RT "Physical mapping of mutations in the structural gene encoding for the
RT Escherichia coli aldohexuronate transport system.";
RL Mol. Gen. Genet. 189:355-357(1983).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
RN [8]
RP FUNCTION AS A D-GLUCOSE TRANSPORTER.
RX PubMed=32038601; DOI=10.3389/fmicb.2020.00027;
RA Kim H.J., Jeong H., Lee S.J.;
RT "Short-term adaptation modulates anaerobic metabolic flux to succinate by
RT activating ExuT, a novel D-glucose transporter in Escherichia coli.";
RL Front. Microbiol. 11:27-27(2020).
CC -!- FUNCTION: Transport of aldohexuronates such as D-glucuronate and D-
CC galacturonate (PubMed:783117, PubMed:6343797). Under anaerobic
CC conditions, can play a critical role as a D-glucose transporter in the
CC absence of sugar-PTS system (PubMed:32038601).
CC {ECO:0000269|PubMed:32038601, ECO:0000269|PubMed:6343797,
CC ECO:0000269|PubMed:783117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-glucuronate(in) + H(+)(in) = aldehydo-D-
CC glucuronate(out) + H(+)(out); Xref=Rhea:RHEA:28955,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:142686;
CC Evidence={ECO:0000305|PubMed:783117};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-galacturonate(out) + H(+)(out) = aldehydo-D-
CC galacturonate(in) + H(+)(in); Xref=Rhea:RHEA:29295,
CC ChEBI:CHEBI:12952, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000305|PubMed:783117};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + H(+)(out) = D-glucose(in) + H(+)(in);
CC Xref=Rhea:RHEA:69556, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000305|PubMed:32038601};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Negatively controlled by ExuR (PubMed:783117). Repressed by
CC H-NS (PubMed:19429622). {ECO:0000269|PubMed:19429622,
CC ECO:0000269|PubMed:783117}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on either glucuronate or
CC galacturonate, but is able to grow on fructuronate or tagaturonate.
CC {ECO:0000269|PubMed:783117}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57897.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA02588.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77143.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D13328; BAA02588.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA57897.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76128.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77143.1; ALT_INIT; Genomic_DNA.
DR PIR; B65098; B65098.
DR RefSeq; NP_417564.2; NC_000913.3.
DR RefSeq; WP_001226465.1; NZ_LN832404.1.
DR AlphaFoldDB; P0AA78; -.
DR SMR; P0AA78; -.
DR BioGRID; 4262409; 14.
DR STRING; 511145.b3093; -.
DR TCDB; 2.A.1.14.2; the major facilitator superfamily (mfs).
DR PaxDb; P0AA78; -.
DR PRIDE; P0AA78; -.
DR EnsemblBacteria; AAC76128; AAC76128; b3093.
DR EnsemblBacteria; BAE77143; BAE77143; BAE77143.
DR GeneID; 58389404; -.
DR GeneID; 947601; -.
DR KEGG; ecj:JW3064; -.
DR KEGG; eco:b3093; -.
DR PATRIC; fig|511145.12.peg.3188; -.
DR EchoBASE; EB2594; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR InParanoid; P0AA78; -.
DR OMA; FYKHPKD; -.
DR BioCyc; EcoCyc:EXUT-MON; -.
DR BioCyc; MetaCyc:EXUT-MON; -.
DR PRO; PR:P0AA78; -.
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:0015134; F:hexuronate transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015736; P:hexuronate transmembrane transport; IMP:EcoCyc.
DR Gene3D; 1.20.1250.20; -; 2.
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 inner membrane; Cell membrane; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..432
FT /note="Hexuronate transporter"
FT /id="PRO_0000121379"
FT TOPO_DOM 33..48
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..99
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..164
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..264
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..317
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 432 AA; 46892 MW; 9C3B2422F2B28ED8 CRC64;
MRKIKGLRWY MIALVTLGTV LGYLTRNTVA AAAPTLMEEL NISTQQYSYI IAAYSAAYTV
MQPVAGYVLD VLGTKIGYAM FAVLWAVFCG ATALAGSWGG LAVARGAVGA AEAAMIPAGL
KASSEWFPAK ERSIAVGYFN VGSSIGAMIA PPLVVWAIVM HSWQMAFIIS GALSFIWAMA
WLIFYKHPRD QKHLTDEERD YIINGQEAQH QVSTAKKMSV GQILRNRQFW GIALPRFLAE
PAWGTFNAWI PLFMFKVYGF NLKEIAMFAW MPMLFADLGC ILGGYLPPLF QRWFGVNLIV
SRKMVVTLGA VLMIGPGMIG LFTNPYVAIM LLCIGGFAHQ ALSGALITLS SDVFGRNEVA
TANGLTGMSA WLASTLFALV VGALADTIGF SPLFAVLAVF DLLGALVIWT VLQNKPAIEV
AQETHNDPAP QH
