UHPT_SALTY
ID UHPT_SALTY Reviewed; 463 AA.
AC P27670;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hexose-6-phosphate:phosphate antiporter {ECO:0000250|UniProtKB:P0AGC0};
GN Name=uhpT; OrderedLocusNames=STM3787;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Mediates the exchange of external hexose 6-phosphate and
CC internal inorganic phosphate. {ECO:0000250|UniProtKB:P0AGC0}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AGC0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: External glucose-6-phosphate induces the expression of the
CC UHP-region.
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; M89480; AAA27246.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22645.1; -; Genomic_DNA.
DR PIR; D41853; D41853.
DR RefSeq; NP_462686.1; NC_003197.2.
DR RefSeq; WP_000879181.1; NC_003197.2.
DR AlphaFoldDB; P27670; -.
DR SMR; P27670; -.
DR STRING; 99287.STM3787; -.
DR PaxDb; P27670; -.
DR EnsemblBacteria; AAL22645; AAL22645; STM3787.
DR GeneID; 1255311; -.
DR KEGG; stm:STM3787; -.
DR PATRIC; fig|99287.12.peg.4007; -.
DR HOGENOM; CLU_001265_31_0_6; -.
DR OMA; GTLMWGY; -.
DR PhylomeDB; P27670; -.
DR BioCyc; SENT99287:STM3787-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IBA:GO_Central.
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 2: Evidence at transcript 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_0000199885"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..60
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..122
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..189
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..297
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..357
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..425
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="P -> A (in Ref. 1; AAA27246)"
FT /evidence="ECO:0000305"
FT CONFLICT 385..386
FT /note="GA -> AL (in Ref. 1; AAA27246)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="G -> A (in Ref. 1; AAA27246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50709 MW; C13398B21CEA92DA CRC64;
MLAFLNQVRK PTLDLPLDVR RKMWFKPFMQ SYLVVFIGYL TMYLIRKNFN IAQNDMISTY
GLSMTELGMI GLGFSITYGV GKTLVSYYAD GKNTKQFLPF MLILSAICML GFSASMGAGS
TSLFLMIAFY ALSGFFQSTG GSCSYSTITK WTPRRKRGTF LGFWNISHNL GGAGAAGVAL
FGANYLFDGH VIGMFIFPSI IALIVGFIGL RFGSDSPESY GLGKAEELFG EEISEEDKET
EENEMTKWQI FVEYVLKNKV IWLLCFSNIF LYVVRIGIDQ WSTVYAFQEL KLSKEVAIQG
FTLFEVGALV GTLLWGWLSD LANGRRALVA CVALALIIAT LGVYQHASNQ YVYLASLFAL
GFLVFGPQLL IGVAAVGFVP KKAIGAADGI KGTFAYLIGD SFAKLGLGMI ADGTPVFGLT
GWAGTFAALD AAAIGCICLM AMVAVMEERK IRREKKIQQV NIA
