ID   UVRY_ECOL6              Reviewed;         218 AA.
AC   P66797; Q8XBD4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Response regulator UvrY;
GN   Name=uvrY; OrderedLocusNames=c2327;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Member of the two-component regulatory system UvrY/BarA
CC       involved in the regulation of carbon metabolism via the CsrA/CsrB
CC       regulatory system. UvrY activates the transcription of the untranslated
CC       csrB RNA and of barA, in an autoregulatory loop. Mediates the effects
CC       of CsrA on csrB RNA by BarA-dependent and BarA-independent mechanisms
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated and activated by BarA. {ECO:0000250}.
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DR   EMBL; AE014075; AAN80786.1; -; Genomic_DNA.
DR   RefSeq; WP_000611328.1; NC_004431.1.
DR   AlphaFoldDB; P66797; -.
DR   SMR; P66797; -.
DR   STRING; 199310.c2327; -.
DR   EnsemblBacteria; AAN80786; AAN80786; c2327.
DR   KEGG; ecc:c2327; -.
DR   eggNOG; COG2197; Bacteria.
DR   HOGENOM; CLU_000445_90_1_6; -.
DR   OMA; NVLRKTQ; -.
DR   BioCyc; ECOL199310:C2327-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..218
FT                   /note="Response regulator UvrY"
FT                   /id="PRO_0000081294"
FT   DOMAIN          3..119
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          143..208
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   DNA_BIND        167..186
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT   MOD_RES         54
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   218 AA;  23863 MW;  7F2B48720FA2DDB7 CRC64;
     MINVLLVDDH ELVRAGIRRI LEDIKGIKVV GEASCGEDAV KWCRANAVDV VLMDMSMPGI
     GGLEATRKIA RSTADVKIIM LTVHTENPLP AKVMQAGAAG YLSKGAAPQE VVSAIRSVYS
     GQRYIASDIA QQMALSQIEP EKTESPFASL SERELQIMLM ITKGQKVNEI SEQLNLSPKT
     VNSYRYRMFS KLNIHGDVEL THLAIRHGLC NAETLSSQ