GHXP_ECO57
ID GHXP_ECO57 Reviewed; 449 AA.
AC P0AF53; P32702;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Guanine/hypoxanthine permease GhxP;
GN Name=ghxP; Synonyms=yjcD; OrderedLocusNames=Z5663, ECs5046;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: High-affinity transporter for guanine and hypoxanthine.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG59262.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38469.1; -; Genomic_DNA.
DR PIR; B86100; B86100.
DR PIR; F91259; F91259.
DR RefSeq; NP_313073.1; NC_002695.1.
DR RefSeq; WP_000106882.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AF53; -.
DR STRING; 155864.EDL933_5403; -.
DR EnsemblBacteria; AAG59262; AAG59262; Z5663.
DR EnsemblBacteria; BAB38469; BAB38469; ECs_5046.
DR GeneID; 66672020; -.
DR GeneID; 914291; -.
DR KEGG; ece:Z5663; -.
DR KEGG; ecs:ECs_5046; -.
DR PATRIC; fig|386585.9.peg.5270; -.
DR eggNOG; COG2252; Bacteria.
DR HOGENOM; CLU_024508_0_1_6; -.
DR OMA; WVLTNLP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0015205; F:nucleobase transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1904823; P:purine nucleobase transmembrane transport; IEA:UniProt.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR006043; NCS2.
DR PANTHER; PTHR43337; PTHR43337; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..449
FT /note="Guanine/hypoxanthine permease GhxP"
FT /id="PRO_0000169721"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..97
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..109
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..180
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..254
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..314
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..330
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..360
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 386..421
FT /note="Discontinuously helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 45711 MW; BDBFE2F057E45910 CRC64;
MSTPSARTGG SLDAWFKISQ RGSTVRQEVV AGLTTFLAMV YSVIVVPGML GKAGFPPAAV
FVATCLVAGL GSIVMGLWAN LPLAIGCAIS LTAFTAFSLV LGQHISVPVA LGAVFLMGVL
FTVISATGIR SWILRNLPHG VAHGTGIGIG LFLLLIAANG VGLVIKNPLD GLPVALGDFA
TFPVIMSLVG LAVIIGLEKL KVPGGILLTI IGISIVGLIF DPNVHFSGVF AMPSLSDENG
NSLIGSLDIM GALNPVVLPS VLALVMTAVF DATGTIRAVA GQANLLDKDG QIIDGGKALT
TDSMSSVFSG LVGAAPAAVY IESAAGTAAG GKTGLTAITV GVLFLLILFL SPLSYLVPGY
ATAPALMYVG LLMLSNVAKI DFADFVDAMA GLVTAVFIVL TCNIVTGIMI GFATLVIGRL
VSGEWRKLNI GTVVIAVALV TFYAGGWAI
