UACR_ECOLI
ID UACR_ECOLI Reviewed; 592 AA.
AC Q46802; Q2M9X1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Putative uric acid sigma-54-dependent transcriptional regulator UacR {ECO:0000305};
DE AltName: Full=Uric acid regulator {ECO:0000303|PubMed:30885932};
GN Name=uacR {ECO:0000303|PubMed:30885932}; Synonyms=ygeV;
GN OrderedLocusNames=b2869, JW2837;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=30885932; DOI=10.1128/jb.00573-18;
RA Iwadate Y., Kato J.I.;
RT "Identification of a formate-dependent uric acid degradation pathway in
RT Escherichia coli.";
RL J. Bacteriol. 201:E00573-E00573(2019).
CC -!- FUNCTION: Essential for both formate-dependent and formate-independent
CC uric acid degradation. May be directly involved in the transcription of
CC uacF in response to hypoxanthine, xanthine, and uric acid.
CC {ECO:0000269|PubMed:30885932}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes urate-degrading
CC activity. {ECO:0000269|PubMed:30885932}.
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DR EMBL; U28375; AAA83050.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75907.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76935.1; -; Genomic_DNA.
DR PIR; E65070; E65070.
DR RefSeq; NP_417345.1; NC_000913.3.
DR RefSeq; WP_000417791.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46802; -.
DR SMR; Q46802; -.
DR BioGRID; 4261521; 20.
DR BioGRID; 851647; 4.
DR DIP; DIP-12157N; -.
DR IntAct; Q46802; 15.
DR STRING; 511145.b2869; -.
DR jPOST; Q46802; -.
DR PaxDb; Q46802; -.
DR PRIDE; Q46802; -.
DR EnsemblBacteria; AAC75907; AAC75907; b2869.
DR EnsemblBacteria; BAE76935; BAE76935; BAE76935.
DR GeneID; 947320; -.
DR KEGG; ecj:JW2837; -.
DR KEGG; eco:b2869; -.
DR PATRIC; fig|1411691.4.peg.3865; -.
DR EchoBASE; EB2864; -.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_8_1_6; -.
DR InParanoid; Q46802; -.
DR OMA; INVIPID; -.
DR PhylomeDB; Q46802; -.
DR BioCyc; EcoCyc:G7488-MON; -.
DR PRO; PR:Q46802; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019628; P:urate catabolic process; IMP:EcoCyc.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW ATP-binding; DNA-binding; Nucleotide-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..592
FT /note="Putative uric acid sigma-54-dependent
FT transcriptional regulator UacR"
FT /id="PRO_0000081380"
FT DOMAIN 158..229
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 272..502
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 567..585
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 300..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 364..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
SQ SEQUENCE 592 AA; 66096 MW; 7FA13B60A4AB9DDD CRC64;
MELATTQSVL MQIQPTIQRF ARMLASVLQL EVEIVDENLC RVAGTGAYGK FLGRQLSGNS
RLLRHVLETK TEKVVTQSRF DPLCEGCDSK ENCREKAFLG TPVILQDRCV GVISLIAVTH
EQQEHISDNL REFSDYVRHI STIFVSKLLE DQGPGDNISK IFATMIDNMD QGVLVVDDEN
RVQFVNQTAL KTLGVVQNNI IGKPIRFRPL TFESNFTHGH MQHIVSWDDK SELIIGQLHN
IQGRQLFLMA FHQSHTSFSV ANAPDEPHIE QLVGECRVMR QLKRLISRIA PSPSSVMVVG
ESGTGKEVVA RAIHKLSGRR NKPFIAINCA AIPEQLLESE LFGYVKGAFT GASANGKTGL
IQAANTGTLF LDEIGDMPLM LQAKLLRAIE AREILPIGAS SPIQVDIRII SATNQNLAQF
IAEGKFREDL FYRLNVIPIT LPPLRERQED IELLVHYFLH LHTRRLGSVY PGIAPDVVEI
LRKHRWPGNL RELSNLMEYL VNVVPSGEVI DSTLLPPNLL NNGTTEQSDV TEVSEAHLSL
DDAGGTALEE MEKQMIREAL SRHNSKKQVA DELGIGIATL YRKIKKYELL NT
