XAPB_ECOLI
ID XAPB_ECOLI Reviewed; 418 AA.
AC P45562; P77729;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Xanthosine permease {ECO:0000303|PubMed:11466294};
DE AltName: Full=Xanthosine transporter {ECO:0000305};
GN Name=xapB {ECO:0000303|PubMed:7559336}; OrderedLocusNames=b2406, JW2397;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=7559336; DOI=10.1128/jb.177.19.5506-5516.1995;
RA Seeger C., Poulsen C., Dandanell G.;
RT "Identification and characterization of genes (xapA, xapB, and xapR)
RT involved in xanthosine catabolism in Escherichia coli.";
RL J. Bacteriol. 177:5506-5516(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11466294; DOI=10.1128/jb.183.16.4900-4904.2001;
RA Noerholm M.H., Dandanell G.;
RT "Specificity and topology of the Escherichia coli xanthosine permease, a
RT representative of the NHS subfamily of the major facilitator superfamily.";
RL J. Bacteriol. 183:4900-4904(2001).
RN [6]
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).
CC -!- FUNCTION: Uptake of xanthosine (PubMed:11466294). Can also transport
CC other nucleosides such as inosine, adenosine, cytidine, uridine and
CC thymidine (PubMed:11466294). Transport is driven by a proton motive
CC force (PubMed:11466294). {ECO:0000269|PubMed:11466294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + xanthosine(in) = H(+)(out) + xanthosine(out);
CC Xref=Rhea:RHEA:28939, ChEBI:CHEBI:15378, ChEBI:CHEBI:18107;
CC Evidence={ECO:0000269|PubMed:11466294};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28941;
CC Evidence={ECO:0000269|PubMed:11466294};
CC -!- ACTIVITY REGULATION: Transport is abolished by the proton uncoupler
CC 2,4-dinitrophenol. {ECO:0000269|PubMed:11466294}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=136 uM for xanthosine {ECO:0000269|PubMed:11466294};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11466294,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:7559336}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant grows very slowly on xanthosine.
CC {ECO:0000269|PubMed:7559336}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Nucleoside:H(+) symporter (NHS) (TC 2.A.1.10) family. {ECO:0000305}.
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DR EMBL; X73828; CAA52048.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75459.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16274.1; -; Genomic_DNA.
DR PIR; E65014; E65014.
DR RefSeq; NP_416901.1; NC_000913.3.
DR RefSeq; WP_000020402.1; NZ_LN832404.1.
DR AlphaFoldDB; P45562; -.
DR SMR; P45562; -.
DR BioGRID; 4262006; 20.
DR STRING; 511145.b2406; -.
DR TCDB; 2.A.1.10.2; the major facilitator superfamily (mfs).
DR PaxDb; P45562; -.
DR PRIDE; P45562; -.
DR EnsemblBacteria; AAC75459; AAC75459; b2406.
DR EnsemblBacteria; BAA16274; BAA16274; BAA16274.
DR GeneID; 946868; -.
DR KEGG; ecj:JW2397; -.
DR KEGG; eco:b2406; -.
DR PATRIC; fig|1411691.4.peg.4326; -.
DR EchoBASE; EB2951; -.
DR eggNOG; COG2211; Bacteria.
DR HOGENOM; CLU_013133_1_2_6; -.
DR InParanoid; P45562; -.
DR OMA; FWVMLIN; -.
DR PhylomeDB; P45562; -.
DR BioCyc; EcoCyc:XAPB-MON; -.
DR BioCyc; MetaCyc:XAPB-MON; -.
DR PRO; PR:P45562; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; ISS:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015212; F:cytidine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; ISA:EcoliWiki.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015553; F:xanthosine transmembrane transporter activity; ISS:EcoliWiki.
DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; IMP:EcoliWiki.
DR GO; GO:0015858; P:nucleoside transport; ISA:EcoliWiki.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004740; Nuc_H_symport.
DR Pfam; PF03825; Nuc_H_symport; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00889; 2A0110; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..418
FT /note="Xanthosine permease"
FT /id="PRO_0000066003"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..41
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..159
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..254
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..306
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..381
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:11466294"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000305|PubMed:11466294"
FT CONFLICT 63..80
FT /note="DKWLRAERAYMLCHLVCA -> VQMRARRTCIHAVSPGVC (in Ref. 1;
FT CAA52048)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..299
FT /note="LRFGFFA -> CALASSP (in Ref. 1; CAA52048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46140 MW; C056971AE8A719E8 CRC64;
MSIAMRLKVM SFLQYFIWGS WLVTLGSYMI NTLHFTGANV GMVYSSKGIA AIIMPGIMGI
IADKWLRAER AYMLCHLVCA GVLFYAASVT DPDMMFWVML VNAMAFMPTI ALSNSVSYSC
LAQAGLDPVT AFPPIRVFGT VGFIVAMWAV SLLHLELSSL QLYIASGASL LLSAYALTLP
KIPVAEKKAT TSLASKLGLD AFVLFKNPRM AIFFLFAMML GAVLQITNVF GNPFLHDFAR
NPEFADSFVV KYPSILLSVS QMAEVGFILT IPFFLKRFGI KTVMLMSMVA WTLRFGFFAY
GDPSTTGFIL LLLSMIVYGC AFDFFNISGS VFVEQEVDSS IRASAQGLFM TMVNGVGAWV
GSILSGMAVD YFSVDGVKDW QTIWLVFAGY ALFLAVIFFF GFKYNHDPEK IKHRAVTH
