URAA_ECO57
ID URAA_ECO57 Reviewed; 429 AA.
AC P0AGM8; P33780;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Uracil permease {ECO:0000250|UniProtKB:P0AGM7};
DE AltName: Full=Uracil transporter {ECO:0000250|UniProtKB:P0AGM7};
DE AltName: Full=Uracil/H(+) symporter UraA {ECO:0000250|UniProtKB:P0AGM7};
GN Name=uraA; OrderedLocusNames=Z3760, ECs3359;
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: Transport of uracil in the cell.
CC {ECO:0000250|UniProtKB:P0AGM7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + uracil(in) = H(+)(out) + uracil(out);
CC Xref=Rhea:RHEA:29239, ChEBI:CHEBI:15378, ChEBI:CHEBI:17568;
CC Evidence={ECO:0000250|UniProtKB:P0AGM7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29241;
CC Evidence={ECO:0000250|UniProtKB:P0AGM7};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AGM7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0AGM7}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57607.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36782.1; -; Genomic_DNA.
DR PIR; C85893; C85893.
DR PIR; G91048; G91048.
DR RefSeq; NP_311386.1; NC_002695.1.
DR RefSeq; WP_000198328.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AGM8; -.
DR SMR; P0AGM8; -.
DR STRING; 155864.EDL933_3652; -.
DR EnsemblBacteria; AAG57607; AAG57607; Z3760.
DR EnsemblBacteria; BAB36782; BAB36782; ECs_3359.
DR GeneID; 66673638; -.
DR GeneID; 915224; -.
DR KEGG; ece:Z3760; -.
DR KEGG; ecs:ECs_3359; -.
DR PATRIC; fig|386585.9.peg.3508; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_1_2_6; -.
DR OMA; INHGIGM; -.
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:UniProt.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR006042; Xan_ur_permease.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR TIGRFAMs; TIGR00801; ncs2; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..429
FT /note="Uracil permease"
FT /id="PRO_0000165959"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 14..37
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 38..41
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 42..61
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 62..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 65..81
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 82..89
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 111..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 145..155
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 156..171
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 172..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 200..224
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 249..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 282..298
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 299..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 302..319
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 320..332
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 355..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT INTRAMEM 366..401
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 402..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT BINDING 73
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT BINDING 241
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT BINDING 289
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT BINDING 290
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
SQ SEQUENCE 429 AA; 45060 MW; 18045190C960C674 CRC64;
MTRRAIGVSE RPPLLQTIPL SLQHLFAMFG ATVLVPVLFH INPATVLLFN GIGTLLYLFI
CKGKIPAYLG SSFAFISPVL LLLPLGYEVA LGGFIMCGVL FCLVSFIVKK AGTGWLDVLF
PPAAMGAIVA VIGLELAGVA AGMAGLLPAE GQTPDSKTII ISITTLAVTV LGSVLFRGFL
AIIPILIGVL VGYALSFAMG IVDTTPIINA HWFALPTLYT PRFEWFAILT ILPAALVVIA
EHVGHLVVTA NIVKKDLLRD PGLHRSMFAN GLSTVISGFF GSTPNTTYGE NIGVMAITRV
YSTWVIGGAA IFAILLSCVG KLAAAIQMIP LPVMGGVSLL LYGVIGASGI RVLIESKVDY
NKAQNLILTS VILIIGVSGA KVNIGAAELK GMALATIVGI GLSLIFKLIS VLRPEEVVLD
AEDADITDK
