XANQ_ECOLI
ID XANQ_ECOLI Reviewed; 466 AA.
AC P67444; Q2M9V8; Q46815;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Xanthine permease XanQ {ECO:0000305};
GN Name=xanQ; Synonyms=ygfO; OrderedLocusNames=b2882, JW2850;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=16096267; DOI=10.1080/09687860500092927;
RA Karatza P., Frillingos S.;
RT "Cloning and functional characterization of two bacterial members of the
RT NAT/NCS2 family in Escherichia coli.";
RL Mol. Membr. Biol. 22:251-261(2005).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND 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 [5]
RP MUTAGENESIS OF PRO-421; SER-423; ILE-424; TYR-425; LEU-427; ASN-430;
RP ILE-432 AND GLY-436.
RC STRAIN=K12;
RX PubMed=18359771; DOI=10.1074/jbc.m800261200;
RA Papakostas K., Georgopoulou E., Frillingos S.;
RT "Cysteine-scanning analysis of putative helix XII in the YgfO xanthine
RT permease: ILE-432 and ASN-430 are important.";
RL J. Biol. Chem. 283:13666-13678(2008).
RN [6]
RP MUTAGENESIS OF HIS-31; ASN-93; LYS-164; ASP-232; GLN-258; GLU-272; ASP-304
RP AND ARG-385.
RC STRAIN=K12;
RX PubMed=19581302; DOI=10.1074/jbc.m109.030734;
RA Karena E., Frillingos S.;
RT "Role of intramembrane polar residues in the YgfO xanthine permease: HIS-31
RT and ASN-93 are crucial for affinity and specificity, and ASP-304 and GLU-
RT 272 are irreplaceable.";
RL J. Biol. Chem. 284:24257-24268(2009).
CC -!- FUNCTION: Specific, proton motive force-dependent high-affinity
CC transporter for xanthine. {ECO:0000269|PubMed:16096267}.
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:0000269|PubMed:16096267};
CC -!- ACTIVITY REGULATION: Inhibited by CCCP and N-ethylmaleimide.
CC {ECO:0000269|PubMed:16096267}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 uM for xanthine {ECO:0000269|PubMed:16096267};
CC Vmax=6.36 nmol/min/mg enzyme {ECO:0000269|PubMed:16096267};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:16096267}; 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=AAA83063.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28375; AAA83063.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75920.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76948.1; -; Genomic_DNA.
DR PIR; B65072; B65072.
DR RefSeq; NP_417358.2; NC_000913.3.
DR RefSeq; WP_001280192.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P67444; -.
DR SMR; P67444; -.
DR BioGRID; 4261448; 22.
DR STRING; 511145.b2882; -.
DR TCDB; 2.A.40.4.3; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; P67444; -.
DR PRIDE; P67444; -.
DR DNASU; 949075; -.
DR EnsemblBacteria; AAC75920; AAC75920; b2882.
DR EnsemblBacteria; BAE76948; BAE76948; BAE76948.
DR GeneID; 949075; -.
DR KEGG; ecj:JW2850; -.
DR KEGG; eco:b2882; -.
DR PATRIC; fig|1411691.4.peg.3852; -.
DR EchoBASE; EB2877; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_8_0_6; -.
DR InParanoid; P67444; -.
DR OMA; IKPFFPP; -.
DR PhylomeDB; P67444; -.
DR BioCyc; EcoCyc:YGFO-MON; -.
DR BioCyc; MetaCyc:YGFO-MON; -.
DR SABIO-RK; P67444; -.
DR PRO; PR:P67444; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042907; F:xanthine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0042906; P:xanthine transport; IDA:EcoCyc.
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 1: Evidence at protein level;
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_0000165965"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..55
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..120
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..180
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..258
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..342
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..425
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT SITE 31
FT /note="Essential for affinity and specificity"
FT SITE 93
FT /note="Essential for affinity and specificity"
FT SITE 272
FT /note="Essential for purine uptake"
FT SITE 304
FT /note="Essential for purine uptake"
FT SITE 430
FT /note="Important for purine uptake and affinity"
FT SITE 432
FT /note="Important for purine uptake and affinity"
FT MUTAGEN 31
FT /note="H->C,L: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 31
FT /note="H->K,R: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 31
FT /note="H->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 31
FT /note="H->Q: Increase of activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 93
FT /note="N->A: Highly active."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 93
FT /note="N->C,D,T: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 93
FT /note="N->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 93
FT /note="N->S: Increase of activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 164
FT /note="K->C,R: Highly active."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 232
FT /note="D->C: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 232
FT /note="D->E: Highly active."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 258
FT /note="Q->C: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 258
FT /note="Q->N: Highly active."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 272
FT /note="E->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 272
FT /note="E->D: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 304
FT /note="D->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 304
FT /note="D->E: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 385
FT /note="R->C: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 385
FT /note="R->K: Highly active."
FT /evidence="ECO:0000269|PubMed:19581302"
FT MUTAGEN 421
FT /note="P->C: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 421
FT /note="P->G: Highly active."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 423
FT /note="S->C: Highly active."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 424
FT /note="I->C: Highly active."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 425
FT /note="Y->C: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 427
FT /note="L->C: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 430
FT /note="N->T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 432
FT /note="I->A,S,T,V: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 432
FT /note="I->L,M,E,F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 432
FT /note="I->N,Q: Highly active."
FT /evidence="ECO:0000269|PubMed:18359771"
FT MUTAGEN 436
FT /note="G->C: Highly active."
FT /evidence="ECO:0000269|PubMed:18359771"
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
