URAA_ECOLI
ID URAA_ECOLI Reviewed; 429 AA.
AC P0AGM7; P33780;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Uracil permease {ECO:0000305};
DE AltName: Full=Uracil transporter {ECO:0000303|PubMed:7721693};
DE AltName: Full=Uracil/H(+) symporter UraA {ECO:0000303|PubMed:21423164};
GN Name=uraA {ECO:0000303|PubMed:7721693}; OrderedLocusNames=b2497, JW2482;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=7721693; DOI=10.1128/jb.177.8.2008-2013.1995;
RA Andersen P.S., Frees D., Fast R., Mygind B.;
RT "Uracil uptake in Escherichia coli K-12: isolation of uraA mutants and
RT cloning of the gene.";
RL J. Bacteriol. 177:2008-2013(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP 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).
RN [6] {ECO:0007744|PDB:3QE7}
RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) IN COMPLEX WITH URACIL, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP PHE-73; GLU-241; HIS-245; TYR-288; GLU-290; ASN-291 AND TYR-342.
RX PubMed=21423164; DOI=10.1038/nature09885;
RA Lu F., Li S., Jiang Y., Jiang J., Fan H., Lu G., Deng D., Dang S.,
RA Zhang X., Wang J., Yan N.;
RT "Structure and mechanism of the uracil transporter UraA.";
RL Nature 472:243-246(2011).
CC -!- FUNCTION: Transport of uracil in the cell.
CC {ECO:0000269|PubMed:21423164, ECO:0000269|PubMed:7721693}.
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:0000269|PubMed:21423164};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29241;
CC Evidence={ECO:0000269|PubMed:21423164};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:21423164}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21423164}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant exhibits normal UPRTase activity
CC and cytosine uptake, but defective uracil uptake.
CC {ECO:0000269|PubMed:7721693}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; X73586; CAA51992.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75550.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16385.1; -; Genomic_DNA.
DR PIR; A56265; A56265.
DR RefSeq; NP_416992.1; NC_000913.3.
DR RefSeq; WP_000198328.1; NZ_STEB01000011.1.
DR PDB; 3QE7; X-ray; 2.78 A; A=1-429.
DR PDBsum; 3QE7; -.
DR AlphaFoldDB; P0AGM7; -.
DR SMR; P0AGM7; -.
DR BioGRID; 4261437; 11.
DR DIP; DIP-11094N; -.
DR IntAct; P0AGM7; 1.
DR STRING; 511145.b2497; -.
DR TCDB; 2.A.40.1.1; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; P0AGM7; -.
DR PRIDE; P0AGM7; -.
DR DNASU; 946978; -.
DR EnsemblBacteria; AAC75550; AAC75550; b2497.
DR EnsemblBacteria; BAA16385; BAA16385; BAA16385.
DR GeneID; 66673638; -.
DR GeneID; 946978; -.
DR KEGG; ecj:JW2482; -.
DR KEGG; eco:b2497; -.
DR PATRIC; fig|1411691.4.peg.4242; -.
DR EchoBASE; EB2050; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_1_2_6; -.
DR InParanoid; P0AGM7; -.
DR OMA; INHGIGM; -.
DR PhylomeDB; P0AGM7; -.
DR BioCyc; EcoCyc:URAA-MON; -.
DR BioCyc; MetaCyc:URAA-MON; -.
DR PRO; PR:P0AGM7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015210; F:uracil transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015505; F:uracil:cation symporter activity; IDA:EcoCyc.
DR GO; GO:0098721; P:uracil import across plasma membrane; IDA:EcoCyc.
DR GO; GO:0015857; P:uracil transport; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..429
FT /note="Uracil permease"
FT /id="PRO_0000165958"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 14..37
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 38..41
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 42..61
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 62..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 65..81
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 82..89
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 111..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 145..155
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 156..171
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 172..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 200..224
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 249..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 282..298
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 299..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 302..319
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 320..332
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 355..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT INTRAMEM 366..401
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:21423164"
FT TOPO_DOM 402..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21423164"
FT BINDING 73
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000269|PubMed:21423164"
FT BINDING 241
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000269|PubMed:21423164"
FT BINDING 289
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000269|PubMed:21423164"
FT BINDING 290
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 73
FT /note="F->A: Slightly decreased uracil uptake."
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 241
FT /note="E->A: Abolishes uracil uptake. Abolishes uracil
FT binding."
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 245
FT /note="H->A: Abolishes uracil uptake. Abolishes uracil
FT binding."
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 288
FT /note="Y->A: No effect on uracil uptake."
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 290
FT /note="E->A: Abolishes uracil uptake. Abolishes uracil
FT binding."
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 291
FT /note="N->A: Slightly decreased uracil uptake."
FT /evidence="ECO:0000269|PubMed:21423164"
FT MUTAGEN 342
FT /note="Y->A: Slightly decreased uracil uptake."
FT /evidence="ECO:0000269|PubMed:21423164"
FT HELIX 14..37
FT /evidence="ECO:0007829|PDB:3QE7"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:3QE7"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3QE7"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 87..109
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 156..174
FT /evidence="ECO:0007829|PDB:3QE7"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3QE7"
FT TURN 178..182
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 183..201
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 233..253
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 263..280
FT /evidence="ECO:0007829|PDB:3QE7"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 331..355
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 363..378
FT /evidence="ECO:0007829|PDB:3QE7"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3QE7"
FT HELIX 391..406
FT /evidence="ECO:0007829|PDB:3QE7"
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
