ID A0A0P9CAY7_9BACL Unreviewed; 431 AA.
AC A0A0P9CAY7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Uracil/xanthine transporter {ECO:0008006|Google:ProtNLM};
GN ORFNames=AN477_16560 {ECO:0000313|EMBL:KPV42598.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV42598.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV42598.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV42598.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000256|ARBA:ARBA00008821}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV42598.1}.
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DR EMBL; LJCO01000072; KPV42598.1; -; Genomic_DNA.
DR RefSeq; WP_054970287.1; NZ_LJCO01000072.1.
DR AlphaFoldDB; A0A0P9CAY7; -.
DR STRING; 471514.AN477_16560; -.
DR PATRIC; fig|471514.4.peg.1165; -.
DR OrthoDB; 5597247at2; -.
DR Proteomes; UP000050482; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IEA:UniProt.
DR InterPro; IPR006043; NCS2.
DR NCBIfam; NF037981; NCS2_1; 1.
DR PANTHER; PTHR42810; PURINE PERMEASE C1399.01C-RELATED; 1.
DR PANTHER; PTHR42810:SF1; PURINE PERMEASE YWDJ-RELATED; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050482};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 431 AA; 45459 MW; A5D692E1FDDBF054 CRC64;
MGKQSTTTTT IFAAIQWLGF MFANTVVIPL SVGAAFHMSP VALSGAMARS FMITGIACLI
QGMIGHRLPL MEGQSGLWWG VLLNLAATGS AAGLGISEIG GSVAVGMILG GLALMLAGAF
GLHKFLNRLF TPIVMAVLLL LLAAQLIDIF FEGMMGLNQG HIILPKVALL SLLLVVLVSY
LTIGVRGVVS NFSILIGLAL GWVVYDVWIG GTSSVALPEW SEITRLFAWG KPAYSAGILI
ACVITALINT TNTIATLRAA EPVFDVQIND SIYRRSLLFS GAFTVISGPL SLVAYAPYTS
SIGFLRTTRI LARAPFLLGA ALFVVLGAVP HLAAWFATLP VSVGDSVLFV AYLQLFGSAL
QNIRGIEFNF RTIFRLAPAV LTGLAVLATP KAAFSSLPPI AQSILGNGML DGIILATVLE
AVIPWERLNQ A
//
