XANQ_ECO57
ID XANQ_ECO57 Reviewed; 466 AA.
AC P67446; Q46815;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Xanthine permease XanQ {ECO:0000250|UniProtKB:P67444};
GN Name=xanQ; OrderedLocusNames=Z4221, ECs3755;
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: Specific, proton motive force-dependent high-affinity
CC transporter for xanthine. {ECO:0000250|UniProtKB:P67444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + xanthine(in) = H(+)(out) + xanthine(out);
CC Xref=Rhea:RHEA:29663, ChEBI:CHEBI:15378, ChEBI:CHEBI:17712;
CC Evidence={ECO:0000250|UniProtKB:P67444};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P67444}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58011.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB37178.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58011.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37178.1; ALT_INIT; Genomic_DNA.
DR PIR; C91098; C91098.
DR PIR; G85943; G85943.
DR RefSeq; NP_311782.1; NC_002695.1.
DR RefSeq; WP_001280192.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P67446; -.
DR SMR; P67446; -.
DR STRING; 155864.EDL933_4083; -.
DR EnsemblBacteria; AAG58011; AAG58011; Z4221.
DR EnsemblBacteria; BAB37178; BAB37178; ECs_3755.
DR GeneID; 916416; -.
DR KEGG; ece:Z4221; -.
DR KEGG; ecs:ECs_3755; -.
DR PATRIC; fig|386585.9.peg.3917; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_8_0_6; -.
DR OMA; IKPFFPP; -.
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 InterPro; IPR006043; NCS2.
DR InterPro; IPR006042; Xan_ur_permease.
DR InterPro; IPR029938; XanQ.
DR PANTHER; PTHR42810:SF5; PTHR42810:SF5; 1.
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;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..466
FT /note="Xanthine permease XanQ"
FT /id="PRO_0000165967"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..74
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..139
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..199
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..277
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..361
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..444
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P67444"
SQ SEQUENCE 466 AA; 49108 MW; 95EAFB06FEEE9175 CRC64;
MSDINHAGSD LIFELEDRPP FHQALVGAIT HLLAIFVPMV TPALIVGAAL QLSAETTAYL
VSMAMIASGI GTWLQVNRYG IVGSGLLSIQ SVNFSFVTVM IALGSSMKSD GFHEELIMSS
LLGVSFVGAF LVVGSSFILP YLRRVITPTV SGIVVLMIGL SLIKVGIIDF GGGFAAKSSG
TFGNYEHLGV GLLVLIVVIG FNCCRSPLLR MGGIAIGLCV GYIASLCLGM VDFSSMRNLP
LITIPHPFKY GFSFSFHQFL VVGTIYLLSV LEAVGDITAT AMVSRRPIQG EEYQSRLKGG
VLADGLVSVI ASAVGSLPLT TFAQNNGVIQ MTGVASRYVG RTIAVMLVIL GLFPMIGGFF
TTIPSAVLGG AMTLMFSMIA IAGIRIIITN GLKRRETLIV ATSLGLGLGV SYDPEIFKIL
PASIYVLVEN PICAGGLTAI LLNIILPGGY RQENVLPGIT SAEEMD
