UHPT_ECOLI
ID UHPT_ECOLI Reviewed; 463 AA.
AC P0AGC0; P13408; P76727; Q2M7X9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Hexose-6-phosphate:phosphate antiporter {ECO:0000305};
GN Name=uhpT; OrderedLocusNames=b3666, JW3641;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3301805; DOI=10.1128/jb.169.8.3556-3563.1987;
RA Friedrich M.J., Kadner R.J.;
RT "Nucleotide sequence of the uhp region of Escherichia coli.";
RL J. Bacteriol. 169:3556-3563(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1569007; DOI=10.1128/jb.174.9.2754-2762.1992;
RA Island M.D., Wei B.-Y., Kadner R.J.;
RT "Structure and function of the uhp genes for the sugar phosphate transport
RT system in Escherichia coli and Salmonella typhimurium.";
RL J. Bacteriol. 174:2754-2762(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=5330662; DOI=10.1016/0304-4165(66)90170-x;
RA Winkler H.H.;
RT "A hexose-phosphate transport system in Escherichia coli.";
RL Biochim. Biophys. Acta 117:231-240(1966).
RN [7]
RP INDUCTION.
RX PubMed=4905309; DOI=10.1128/jb.101.2.470-475.1970;
RA Winkler H.H.;
RT "Compartmentation in the induction of the hexose-6-phosphate transport
RT system of Escherichia coli.";
RL J. Bacteriol. 101:470-475(1970).
RN [8]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=3522583; DOI=10.1016/s0021-9258(18)67617-3;
RA Ambudkar S.V., Larson T.J., Maloney P.C.;
RT "Reconstitution of sugar phosphate transport systems of Escherichia coli.";
RL J. Biol. Chem. 261:9083-9086(1986).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=3038843; DOI=10.1128/jb.169.8.3546-3555.1987;
RA Weston L.A., Kadner R.J.;
RT "Identification of uhp polypeptides and evidence for their role in
RT exogenous induction of the sugar phosphate transport system of Escherichia
RT coli K-12.";
RL J. Bacteriol. 169:3546-3555(1987).
RN [10]
RP FUNCTION AS AN HEXOSE-6-PHOSPHATE:PHOSPHATE ANTIPORTER, AND ACTIVITY
RP REGULATION.
RX PubMed=3283129; DOI=10.1016/s0021-9258(18)68687-9;
RA Sonna L.A., Ambudkar S.V., Maloney P.C.;
RT "The mechanism of glucose 6-phosphate transport by Escherichia coli.";
RL J. Biol. Chem. 263:6625-6630(1988).
RN [11]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=2156798; DOI=10.1128/jb.172.4.1688-1693.1990;
RA Lloyd A.D., Kadner R.J.;
RT "Topology of the Escherichia coli uhpT sugar-phosphate transporter analyzed
RT by using TnphoA fusions.";
RL J. Bacteriol. 172:1688-1693(1990).
RN [12]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=2197272; DOI=10.1016/s0021-9258(19)38343-7;
RA Ambudkar S.V., Anantharam V., Maloney P.C.;
RT "UhpT, the sugar phosphate antiporter of Escherichia coli, functions as a
RT monomer.";
RL J. Biol. Chem. 265:12287-12292(1990).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYS-108;
RP CYS-143; CYS-265; CYS-331; CYS-436 AND CYS-438.
RX PubMed=8402899; DOI=10.1016/s0092-8674(05)80082-0;
RA Yan R.T., Maloney P.C.;
RT "Identification of a residue in the translocation pathway of a membrane
RT carrier.";
RL Cell 75:37-44(1993).
RN [14]
RP INDUCTION.
RX PubMed=8999880; DOI=10.1074/jbc.272.3.1910;
RA Dahl J.L., Wei B.Y., Kadner R.J.;
RT "Protein phosphorylation affects binding of the Escherichia coli
RT transcription activator UhpA to the uhpT promoter.";
RL J. Biol. Chem. 272:1910-1919(1997).
RN [15]
RP INDUCTION.
RX PubMed=11739766; DOI=10.1099/00221287-147-12-3345;
RA Verhamme D.T., Arents J.C., Postma P.W., Crielaard W., Hellingwerf K.J.;
RT "Glucose-6-phosphate-dependent phosphoryl flow through the Uhp two-
RT component regulatory system.";
RL Microbiology 147:3345-3352(2001).
RN [16]
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).
CC -!- FUNCTION: Mediates the exchange of external hexose 6-phosphate and
CC internal inorganic phosphate. Can transport glucose-6-phosphate,
CC fructose-6-phosphate and mannose-6-phosphate. Also catalyzes the
CC neutral exchange of internal and external phosphate.
CC {ECO:0000269|PubMed:2197272, ECO:0000269|PubMed:3038843,
CC ECO:0000269|PubMed:3283129, ECO:0000269|PubMed:3522583,
CC ECO:0000269|PubMed:5330662, ECO:0000269|PubMed:8402899}.
CC -!- ACTIVITY REGULATION: Reaction is unaffected by the ionophores
CC valinomycin, valinomycin plus nigericin, and carbonyl cyanide p-
CC trifluoromethoxyphenylhydrazone (FCCP). {ECO:0000269|PubMed:3283129}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2197272}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2156798, ECO:0000269|PubMed:8402899}; Multi-pass
CC membrane protein {ECO:0000255, ECO:0000269|PubMed:2156798}.
CC -!- INDUCTION: Expression is induced by external glucose-6-phosphate
CC through the UhpABC signaling cascade. {ECO:0000269|PubMed:11739766,
CC ECO:0000269|PubMed:3038843, ECO:0000269|PubMed:4905309,
CC ECO:0000269|PubMed:8999880}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. {ECO:0000305}.
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DR EMBL; M17102; AAA24723.1; -; Genomic_DNA.
DR EMBL; M89479; AAA24727.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62018.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76689.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77627.1; -; Genomic_DNA.
DR PIR; A30395; MMECHP.
DR RefSeq; NP_418122.1; NC_000913.3.
DR RefSeq; WP_000879194.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P0AGC0; -.
DR SMR; P0AGC0; -.
DR BioGRID; 4262581; 5.
DR STRING; 511145.b3666; -.
DR TCDB; 2.A.1.4.1; the major facilitator superfamily (mfs).
DR PaxDb; P0AGC0; -.
DR PRIDE; P0AGC0; -.
DR EnsemblBacteria; AAC76689; AAC76689; b3666.
DR EnsemblBacteria; BAE77627; BAE77627; BAE77627.
DR GeneID; 66672437; -.
DR GeneID; 948201; -.
DR KEGG; ecj:JW3641; -.
DR KEGG; eco:b3666; -.
DR PATRIC; fig|1411691.4.peg.3039; -.
DR EchoBASE; EB1047; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_31_0_6; -.
DR InParanoid; P0AGC0; -.
DR OMA; GTLMWGY; -.
DR PhylomeDB; P0AGC0; -.
DR BioCyc; EcoCyc:UHPT-MON; -.
DR BioCyc; MetaCyc:UHPT-MON; -.
DR PRO; PR:P0AGC0; -.
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:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IBA:GO_Central.
DR GO; GO:0015526; F:hexose-phosphate:inorganic phosphate antiporter activity; IDA:EcoCyc.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IDA:EcoCyc.
DR GO; GO:0015712; P:hexose phosphate transport; IMP:EcoCyc.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR021159; Sugar-P_transporter_CS.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS00942; GLPT; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Phosphate transport;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..463
FT /note="Hexose-6-phosphate:phosphate antiporter"
FT /id="PRO_0000199883"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..60
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..120
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2156798,
FT ECO:0000305|PubMed:8402899"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..189
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..297
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2156798"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..357
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2156798"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 392..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..425
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2156798"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000305|PubMed:2156798"
FT MUTAGEN 108
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:8402899"
FT MUTAGEN 143
FT /note="C->S: 30% of wild-type sugar phosphate transport
FT activity."
FT /evidence="ECO:0000269|PubMed:8402899"
FT MUTAGEN 265
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:8402899"
FT MUTAGEN 331
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:8402899"
FT MUTAGEN 436
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:8402899"
FT MUTAGEN 438
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:8402899"
SQ SEQUENCE 463 AA; 50607 MW; 1BE23CEFF05311B6 CRC64;
MLAFLNQVRK PTLDLPLEVR RKMWFKPFMQ SYLVVFIGYL TMYLIRKNFN IAQNDMISTY
GLSMTQLGMI GLGFSITYGV GKTLVSYYAD GKNTKQFLPF MLILSAICML GFSASMGSGS
VSLFLMIAFY ALSGFFQSTG GSCSYSTITK WTPRRKRGTF LGFWNISHNL GGAGAAGVAL
FGANYLFDGH VIGMFIFPSI IALIVGFIGL RYGSDSPESY GLGKAEELFG EEISEEDKET
ESTDMTKWQI FVEYVLKNKV IWLLCFANIF LYVVRIGIDQ WSTVYAFQEL KLSKAVAIQG
FTLFEAGALV GTLLWGWLSD LANGRRGLVA CIALALIIAT LGVYQHASNE YIYLASLFAL
GFLVFGPQLL IGVAAVGFVP KKAIGAADGI KGTFAYLIGD SFAKLGLGMI ADGTPVFGLT
GWAGTFAALD IAAIGCICLM AIVAVMEERK IRREKKIQQL TVA
