ID UACT_ECOLI Reviewed; 482 AA.
AC Q46821; Q2M9V3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Uric acid transporter UacT;
GN Name=uacT; Synonyms=ygfU; OrderedLocusNames=b2888, JW5470;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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 TOPOLOGY [LARGE SCALE ANALYSIS].
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 [4]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, GENE NAME, AND MUTAGENESIS OF HIS-37; THR-100; SER-256; THR-259;
RP GLU-270; LEU-278; ASP-298; SER-317; GLN-318; ASN-319; VAL-320; ARG-327 AND
RP SER-426.
RC STRAIN=K12;
RX PubMed=22437829; DOI=10.1074/jbc.m112.355818;
RA Papakostas K., Frillingos S.;
RT "Substrate selectivity of YgfU, a uric acid transporter from Escherichia
RT coli.";
RL J. Biol. Chem. 287:15684-15695(2012).
CC -!- FUNCTION: Proton-dependent high-capacity transporter for uric acid.
CC Shows also a low capacity for transport of xanthine at 37 degrees
CC Celsius but not at 25 degrees Celsius. {ECO:0000269|PubMed:22437829}.
CC -!- ACTIVITY REGULATION: Inhibited in the presence of the protonophore
CC carbonyl cyanide m-chlorophenyl hydrazone.
CC {ECO:0000269|PubMed:22437829}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for uric acid {ECO:0000269|PubMed:22437829};
CC KM=0.3 mM for xanthine {ECO:0000269|PubMed:22437829};
CC Vmax=715 nmol/min/mg enzyme with acid uric as substrate
CC {ECO:0000269|PubMed:22437829};
CC Vmax=14 nmol/min/mg enzyme with xanthine as substrate (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:22437829};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22437829}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22437829}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83069.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U28375; AAA83069.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75926.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76953.1; -; Genomic_DNA.
DR PIR; H65072; H65072.
DR RefSeq; NP_417364.2; NC_000913.3.
DR RefSeq; WP_001295374.1; NZ_SSZK01000003.1.
DR AlphaFoldDB; Q46821; -.
DR SMR; Q46821; -.
DR BioGRID; 4262336; 163.
DR DIP; DIP-12176N; -.
DR STRING; 511145.b2888; -.
DR TCDB; 2.A.40.3.3; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; 511145-b2888; -.
DR DNASU; 949017; -.
DR EnsemblBacteria; AAC75926; AAC75926; b2888.
DR GeneID; 75205276; -.
DR GeneID; 949017; -.
DR KEGG; ecj:JW5470; -.
DR KEGG; eco:b2888; -.
DR PATRIC; fig|1411691.4.peg.3847; -.
DR EchoBASE; EB2882; -.
DR eggNOG; COG2233; Bacteria.
DR HOGENOM; CLU_017959_8_2_6; -.
DR InParanoid; Q46821; -.
DR OMA; AHANSEM; -.
DR OrthoDB; 9805749at2; -.
DR PhylomeDB; Q46821; -.
DR BioCyc; EcoCyc:YGFU-MONOMER; -.
DR BioCyc; MetaCyc:YGFU-MONOMER; -.
DR PRO; PR:Q46821; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015143; F:urate transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042907; F:xanthine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0015747; P:urate transport; IMP:EcoCyc.
DR GO; GO:0042906; P:xanthine transport; IMP:EcoCyc.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR017588; UacT-like.
DR InterPro; IPR006042; Xan_ur_permease.
DR NCBIfam; TIGR00801; ncs2; 1.
DR NCBIfam; NF037981; NCS2_1; 1.
DR NCBIfam; TIGR03173; pbuX; 1.
DR PANTHER; PTHR42810; PURINE PERMEASE C1399.01C-RELATED; 1.
DR PANTHER; PTHR42810:SF4; URIC ACID TRANSPORTER UACT; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..482
FT /note="Uric acid transporter UacT"
FT /id="PRO_0000165968"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..62
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..115
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..178
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..261
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..421
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 37
FT /note="H->K,L: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 37
FT /note="H->N: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 100
FT /note="T->A: Decrease in activity with uric acid. Highly
FT active with xanthine."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 100
FT /note="T->S: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 256
FT /note="S->Q: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 259
FT /note="T->V: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 270
FT /note="E->D,N,Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 278
FT /note="L->T: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 298
FT /note="D->E: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 298
FT /note="D->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 317
FT /note="S->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 318
FT /note="Q->E,N: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 319
FT /note="N->D,Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 320
FT /note="V->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 327
FT /note="R->G: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
FT MUTAGEN 426
FT /note="S->N: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:22437829"
SQ SEQUENCE 482 AA; 51758 MW; E08EF1D4CBD9D066 CRC64;
MSAIDSQLPS SSGQDRPTDE VDRILSPGKL IILGLQHVLV MYAGAVAVPL MIGDRLGLSK
EAIAMLISSD LFCCGIVTLL QCIGIGRFMG IRLPVIMSVT FAAVTPMIAI GMNPDIGLLG
IFGATIAAGF ITTLLAPLIG RLMPLFPPLV TGVVITSIGL SIIQVGIDWA AGGKGNPQYG
NPVYLGISFA VLIFILLITR YAKGFMSNVA VLLGIVFGFL LSWMMNEVNL SGLHDASWFA
IVTPMSFGMP IFDPVSILTM TAVLIIVFIE SMGMFLALGE IVGRKLSSHD IIRGLRVDGV
GTMIGGTFNS FPHTSFSQNV GLVSVTRVHS RWVCISSGII LILFGMVPKM AVLVASIPQF
VLGGAGLVMF GMVLATGIRI LSRCNYTTNR YNLYIVAISL GVGMTPTLSH DFFSKLPAVL
QPLLHSGIML ATLSAVVLNV FFNGYQHHAD LVKESVSDKD LKVRTVRMWL LMRKLKKNEH
GE
//
