UVRY_ECOLI
ID UVRY_ECOLI Reviewed; 218 AA.
AC P0AED5; P07027;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Response regulator UvrY;
GN Name=uvrY; Synonyms=yecB; OrderedLocusNames=b1914, JW1899;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3295776; DOI=10.1093/nar/15.10.4273;
RA Moolenaar G.F., van Sluis C.A., Backendorf C., van de Putte P.;
RT "Regulation of the Escherichia coli excision repair gene uvrC. Overlap
RT between the uvrC structural gene and the region coding for a 24 kD
RT protein.";
RL Nucleic Acids Res. 15:4273-4289(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-218.
RX PubMed=3515318; DOI=10.1093/nar/14.5.2301;
RA Sharma S., Stark T.F., Beattie W.G., Moses R.E.;
RT "Multiple control elements for the uvrC gene unit of Escherichia coli.";
RL Nucleic Acids Res. 14:2301-2318(1986).
RN [6]
RP PHOSPHORYLATION BY BARA, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11022030; DOI=10.1074/jbc.m001550200;
RA Pernestig A.-K., Melefors O., Georgellis D.;
RT "Identification of UvrY as the cognate response regulator for the BarA
RT sensor kinase in Escherichia coli.";
RL J. Biol. Chem. 276:225-231(2001).
RN [7]
RP FUNCTION, ACTIVATION BY BARA, AND INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12193630; DOI=10.1128/jb.184.18.5130-5140.2002;
RA Suzuki K., Wang X., Weilbacher T., Pernestig A.-K., Melefors O.,
RA Georgellis D., Babitzke P., Romeo T.;
RT "Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia
RT coli.";
RL J. Bacteriol. 184:5130-5140(2002).
RN [8]
RP FUNCTION.
RX PubMed=12533459; DOI=10.1128/jb.185.3.843-853.2003;
RA Pernestig A.-K., Georgellis D., Romeo T., Suzuki K., Tomenius H.,
RA Normark S., Melefors O.;
RT "The Escherichia coli BarA-UvrY two-component system is needed for
RT efficient switching between glycolytic and gluconeogenic carbon sources.";
RL J. Bacteriol. 185:843-853(2003).
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 (PubMed:12193630, PubMed:12533459). UvrY activates
CC the transcription of the untranslated csrB RNA and of barA, in an
CC autoregulatory loop. Mediates the effects of CsrA on csrB RNA by BarA-
CC dependent and BarA-independent mechanisms (PubMed:12193630).
CC {ECO:0000269|PubMed:12193630, ECO:0000269|PubMed:12533459}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is regulated by SidA.
CC {ECO:0000269|PubMed:12193630}.
CC -!- PTM: Phosphorylated and activated by BarA.
CC {ECO:0000269|PubMed:11022030, ECO:0000269|PubMed:12193630}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to hydrogen
CC peroxide hypersensitivity. {ECO:0000269|PubMed:11022030}.
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DR EMBL; M24615; AAA24755.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74981.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15734.1; -; Genomic_DNA.
DR EMBL; X05398; CAA28982.1; -; Genomic_DNA.
DR EMBL; X03691; CAA27328.1; -; Genomic_DNA.
DR PIR; A26750; QQEC24.
DR RefSeq; NP_416424.1; NC_000913.3.
DR RefSeq; WP_000611335.1; NZ_STEB01000026.1.
DR AlphaFoldDB; P0AED5; -.
DR SMR; P0AED5; -.
DR BioGRID; 4261107; 103.
DR DIP; DIP-35922N; -.
DR IntAct; P0AED5; 37.
DR STRING; 511145.b1914; -.
DR jPOST; P0AED5; -.
DR PaxDb; P0AED5; -.
DR PRIDE; P0AED5; -.
DR EnsemblBacteria; AAC74981; AAC74981; b1914.
DR EnsemblBacteria; BAA15734; BAA15734; BAA15734.
DR GeneID; 66674197; -.
DR GeneID; 946424; -.
DR KEGG; ecj:JW1899; -.
DR KEGG; eco:b1914; -.
DR PATRIC; fig|1411691.4.peg.336; -.
DR EchoBASE; EB1130; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_000445_90_1_6; -.
DR InParanoid; P0AED5; -.
DR OMA; NVLRKTQ; -.
DR PhylomeDB; P0AED5; -.
DR BioCyc; EcoCyc:EG11140-MON; -.
DR PRO; PR:P0AED5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..218
FT /note="Response regulator UvrY"
FT /id="PRO_0000081292"
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"
FT CONFLICT 8..9
FT /note="DD -> MT (in Ref. 5; CAA27328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23893 MW; 708E52D8BFA97716 CRC64;
MINVLLVDDH ELVRAGIRRI LEDIKGIKVV GEASCGEDAV KWCRTNAVDV VLMDMSMPGI
GGLEATRKIA RSTADVKIIM LTVHTENPLP AKVMQAGAAG YLSKGAAPQE VVSAIRSVYS
GQRYIASDIA QQMALSQIEP EKTESPFASL SERELQIMLM ITKGQKVNEI SEQLNLSPKT
VNSYRYRMFS KLNIHGDVEL THLAIRHGLC NAETLSSQ
