XANP_ECOLI
ID XANP_ECOLI Reviewed; 463 AA.
AC P0AGM9; P27432; Q2M7W7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Xanthine permease XanP {ECO:0000305};
GN Name=xanP; Synonyms=yicE; OrderedLocusNames=b3654, JW3629;
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=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC STRAIN=K12;
RX PubMed=2017136; DOI=10.1007/bf00261677;
RA Kalman M., Gentry D., Cashel M.;
RT "Characterization of the Escherichia coli K12 gltS glutamate permease
RT gene.";
RL Mol. Gen. Genet. 225:379-386(1991).
RN [5]
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).
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=2.9 uM for xanthine {ECO:0000269|PubMed:16096267};
CC Vmax=0.59 nmol/min/mg enzyme {ECO:0000269|PubMed:16096267};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
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}.
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DR EMBL; L10328; AAA62007.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76678.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77639.1; -; Genomic_DNA.
DR EMBL; X17499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H65166; H65166.
DR RefSeq; NP_418111.1; NC_000913.3.
DR RefSeq; WP_001295238.1; NZ_SSZK01000043.1.
DR AlphaFoldDB; P0AGM9; -.
DR SMR; P0AGM9; -.
DR BioGRID; 4262570; 8.
DR STRING; 511145.b3654; -.
DR TCDB; 2.A.40.4.2; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; P0AGM9; -.
DR PRIDE; P0AGM9; -.
DR DNASU; 948172; -.
DR EnsemblBacteria; AAC76678; AAC76678; b3654.
DR EnsemblBacteria; BAE77639; BAE77639; BAE77639.
DR GeneID; 66672450; -.
DR GeneID; 948172; -.
DR KEGG; ecj:JW3629; -.
DR KEGG; eco:b3654; -.
DR PATRIC; fig|511145.12.peg.3774; -.
DR EchoBASE; EB1180; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_8_0_6; -.
DR InParanoid; P0AGM9; -.
DR OMA; RKSAPFF; -.
DR PhylomeDB; P0AGM9; -.
DR BioCyc; EcoCyc:YICE-MON; -.
DR BioCyc; MetaCyc:YICE-MON; -.
DR SABIO-RK; P0AGM9; -.
DR PRO; PR:P0AGM9; -.
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 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..463
FT /note="Xanthine permease XanP"
FT /id="PRO_0000165969"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 48868 MW; 868718559103456E CRC64;
MSVSTLESEN AQPVAQTQNS ELIYRLEDRP PLPQTLFAAC QHLLAMFVAV ITPALLICQA
LGLPAQDTQH IISMSLFASG VASIIQIKAW GPVGSGLLSI QGTSFNFVAP LIMGGTALKT
GGADVPTMMA ALFGTLMLAS CTEMVISRVL HLARRIITPL VSGVVVMIIG LSLIQVGLTS
IGGGYAAMSD NTFGAPKNLL LAGVVLALII LLNRQRNPYL RVASLVIAMA AGYALAWFMG
MLPESNEPMT QELIMVPTPL YYGLGIEWSL LLPLMLVFMI TSLETIGDIT ATSDVSEQPV
SGPLYMKRLK GGVLANGLNS FVSAVFNTFP NSCFGQNNGV IQLTGVASRY VGFVVALMLI
VLGLFPAVSG FVQHIPEPVL GGATLVMFGT IAASGVRIVS REPLNRRAIL IIALSLAVGL
GVSQQPLILQ FAPEWLKNLL SSGIAAGGIT AIVLNLIFPP EKQ
