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URAA_HAEIN
ID   URAA_HAEIN              Reviewed;         414 AA.
AC   P45117;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=HI_1227;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC22880.1; -; Genomic_DNA.
DR   PIR; D64111; D64111.
DR   RefSeq; NP_439383.1; NC_000907.1.
DR   RefSeq; WP_005694289.1; NC_000907.1.
DR   AlphaFoldDB; P45117; -.
DR   SMR; P45117; -.
DR   STRING; 71421.HI_1227; -.
DR   DNASU; 950172; -.
DR   EnsemblBacteria; AAC22880; AAC22880; HI_1227.
DR   KEGG; hin:HI_1227; -.
DR   PATRIC; fig|71421.8.peg.1279; -.
DR   eggNOG; COG2233; Bacteria.
DR   HOGENOM; CLU_017959_1_2_6; -.
DR   OMA; INHGIGM; -.
DR   PhylomeDB; P45117; -.
DR   BioCyc; HINF71421:G1GJ1-1258-MON; -.
DR   Proteomes; UP000000579; 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..414
FT                   /note="Probable uracil permease"
FT                   /id="PRO_0000165960"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TOPO_DOM        39..42
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TRANSMEM        43..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TOPO_DOM        63..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TRANSMEM        66..82
FT                   /note="Discontinuously helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TOPO_DOM        83..91
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TOPO_DOM        113..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TRANSMEM        125..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   TOPO_DOM        147..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..414
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
FT   BINDING         74
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         290
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250|UniProtKB:P0AGM7"
SQ   SEQUENCE   414 AA;  43572 MW;  25361ABC22FE08B7 CRC64;
     MTNQIPPSLA ENQSKLKQSF VGLQMLFVAF GALVLVPLIT GLDSNTALLT AGVGTLLFQF
     CTGKQVPIFL ASSFAFIAPI QYGVQTWGIA TTMGGLAFTG LVYFALSTLV KLRGAEALQR
     FFPPVVVGPV IIIIGMGLAP IAVDMSLGKN SAYAYNDAVL VSMVTLLTTL SVAVFAKGLM
     KLIPIMFGIT AGYILCLFLG LINFQPVIDA PWFSLPKLTT PEFNLEAILY MLPIAIAPAV
     EHVGGIMAIS SVTGKDFLKK PGLHRTLLGD GIATAAASLV GGPPNTTYAE VTGAVMLTRN
     FNPNIMTWAA VWAIAISFCG KVGAFLSTIP TIVMGGIMML VFGSIAVVGM STLIRGKVDV
     TEARNLCIIS VVMTFGIGNM FVDVGNVSLK GISLCAIVAI ILNLVLPKAK NEVE
 
 
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