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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
 
 
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