UHPT_SHIFL
ID UHPT_SHIFL Reviewed; 463 AA.
AC P0AGC2; P13408; P76727;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Hexose-6-phosphate:phosphate antiporter {ECO:0000250|UniProtKB:P0AGC0};
GN Name=uhpT; OrderedLocusNames=SF3795, S3973;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- 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; AE005674; AAN45235.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18961.1; -; Genomic_DNA.
DR RefSeq; NP_709528.1; NC_004337.2.
DR RefSeq; WP_000879194.1; NZ_WPGW01000019.1.
DR AlphaFoldDB; P0AGC2; -.
DR SMR; P0AGC2; -.
DR STRING; 198214.SF3795; -.
DR EnsemblBacteria; AAN45235; AAN45235; SF3795.
DR EnsemblBacteria; AAP18961; AAP18961; S3973.
DR GeneID; 1026108; -.
DR GeneID; 66672437; -.
DR KEGG; sfl:SF3795; -.
DR KEGG; sfx:S3973; -.
DR PATRIC; fig|198214.7.peg.4480; -.
DR HOGENOM; CLU_001265_31_0_6; -.
DR OMA; GTLMWGY; -.
DR OrthoDB; 1345431at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
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_0000199886"
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..120
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..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"
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
