URAA_PASMU
ID URAA_PASMU Reviewed; 417 AA.
AC Q9CPL9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable 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=PM0018;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; AE004439; AAK02102.1; -; Genomic_DNA.
DR RefSeq; WP_010906431.1; NC_002663.1.
DR AlphaFoldDB; Q9CPL9; -.
DR SMR; Q9CPL9; -.
DR STRING; 747.DR93_2061; -.
DR EnsemblBacteria; AAK02102; AAK02102; PM0018.
DR KEGG; pmu:PM0018; -.
DR PATRIC; fig|272843.6.peg.18; -.
DR HOGENOM; CLU_017959_1_2_6; -.
DR OMA; INHGIGM; -.
DR Proteomes; UP000000809; 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..417
FT /note="Probable uracil permease"
FT /id="PRO_0000165961"
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 83..90
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 112..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 146..154
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 155..170
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 171..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 199..223
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 248..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 281..297
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 298..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 319..331
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 354..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT INTRAMEM 365..400
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT TOPO_DOM 401..416
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 240
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"
SQ SEQUENCE 417 AA; 43933 MW; 494D97CEA35CC6C1 CRC64;
MTNQNPPVLL EQNHAKQAFV GLQMLFVAFG ALVLVPLITG LNANTALLTA GIGTLLFQLC
TGRQVPIFLA SSFAFIAPIQ YGVTTWGIAT TMGGLVFTGL VYFALSTLVK IKGAGALQKV
FPPVVVGPVI IIIGMGLAPV AVDMALGKNS TYQYNDAVFV SMATLLTTLG VAVFAKGMMK
LIPIMFGIVV GYILCLFLGL INFQPVIDAP WFSVPEITTP EFKLEAILYL LPIAIAPAVE
HVGGIMAISS VTGKDFLQKP GLHRTLLGDG IATSAASFLG GPPNTTYAEV TGAVMLTRNF
NPKIMTWAAV WAIAISFCGK VGAFLSTIPT IVMGGIMMLV FGSIAVVGMS TLIRGKVDVT
EARNLCIISV VMTFGIGGMF VNFGEVSLKG ISLCAVVAIL LNLILPKAKN TPIEENR