RHAR_ECOLI
ID RHAR_ECOLI Reviewed; 282 AA.
AC P09378; Q2M8K3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 178.
DE RecName: Full=HTH-type transcriptional activator RhaR {ECO:0000255|HAMAP-Rule:MF_01533};
DE AltName: Full=L-rhamnose operon transcriptional activator RhaR {ECO:0000255|HAMAP-Rule:MF_01533};
GN Name=rhaR {ECO:0000255|HAMAP-Rule:MF_01533}; Synonyms=rhaC1;
GN OrderedLocusNames=b3906, JW3877;
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=3316663; DOI=10.1016/0022-2836(87)90405-0;
RA Tobin J.F., Schleif R.F.;
RT "Positive regulation of the Escherichia coli L-rhamnose operon is mediated
RT by the products of tandemly repeated regulatory genes.";
RL J. Mol. Biol. 196:789-799(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 265-282.
RC STRAIN=K12;
RX PubMed=1339463; DOI=10.1099/00221287-138-6-1109;
RA Garcia C., Baldoma L., Badia J., Aguilar J.;
RT "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in
RT Escherichia coli.";
RL J. Gen. Microbiol. 138:1109-1116(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 266-282.
RC STRAIN=K12;
RX PubMed=1551902; DOI=10.1016/s0021-9258(19)50517-8;
RA Tate C.G., Muiry J.A.R., Henderson P.J.F.;
RT "Mapping, cloning, expression, and sequencing of the rhaT gene, which
RT encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium
RT and Escherichia coli.";
RL J. Biol. Chem. 267:6923-6932(1992).
RN [7]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ECL116;
RX PubMed=8230210; DOI=10.1006/jmbi.1993.1565;
RA Egan S.M., Schleif R.F.;
RT "A regulatory cascade in the induction of rhaBAD.";
RL J. Mol. Biol. 234:87-98(1993).
RN [8]
RP FUNCTION.
RX PubMed=8757746; DOI=10.1099/13500872-142-7-1833;
RA Via P., Badia J., Baldoma L., Obradors N., Aguilar J.;
RT "Transcriptional regulation of the Escherichia coli rhaT gene.";
RL Microbiology 142:1833-1840(1996).
RN [9]
RP REGULATION BY CRP.
RX PubMed=11073923; DOI=10.1128/jb.182.23.6774-6782.2000;
RA Holcroft C.C., Egan S.M.;
RT "Interdependence of activation at rhaSR by cyclic AMP receptor protein, the
RT RNA polymerase alpha subunit C-terminal domain, and rhaR.";
RL J. Bacteriol. 182:6774-6782(2000).
RN [10]
RP INTERACTION WITH SIGMA-70.
RX PubMed=15342598; DOI=10.1128/jb.186.18.6277-6285.2004;
RA Wickstrum J.R., Egan S.M.;
RT "Amino acid contacts between sigma 70 domain 4 and the transcription
RT activators RhaS and RhaR.";
RL J. Bacteriol. 186:6277-6285(2004).
CC -!- FUNCTION: Activates expression of the rhaSR operon in response to L-
CC rhamnose. {ECO:0000255|HAMAP-Rule:MF_01533, ECO:0000269|PubMed:8230210,
CC ECO:0000269|PubMed:8757746}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000255|HAMAP-Rule:MF_01533,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01533}.
CC -!- INDUCTION: Autoregulated. Binding of the cAMP receptor protein (CRP) is
CC required for full expression. {ECO:0000269|PubMed:8230210}.
CC -!- MISCELLANEOUS: Its activity is regulated by L-rhamnose. When this sugar
CC becomes available to the cell, basal-level RhaR binds L-rhamnose and
CC becomes activated.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24530.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAB03039.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE77403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA29453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X06058; CAA29453.1; ALT_INIT; Genomic_DNA.
DR EMBL; L19201; AAB03039.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76888.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77403.1; ALT_INIT; Genomic_DNA.
DR EMBL; X60699; CAA43110.1; -; Genomic_DNA.
DR EMBL; M85158; AAA24530.1; ALT_SEQ; Genomic_DNA.
DR PIR; S40850; S40850.
DR RefSeq; NP_418342.2; NC_000913.3.
DR RefSeq; WP_001336056.1; NZ_SSZK01000014.1.
DR AlphaFoldDB; P09378; -.
DR SMR; P09378; -.
DR BioGRID; 4263058; 8.
DR BioGRID; 852693; 3.
DR DIP; DIP-10693N; -.
DR IntAct; P09378; 9.
DR STRING; 511145.b3906; -.
DR PaxDb; P09378; -.
DR PRIDE; P09378; -.
DR EnsemblBacteria; AAC76888; AAC76888; b3906.
DR EnsemblBacteria; BAE77403; BAE77403; BAE77403.
DR GeneID; 948396; -.
DR KEGG; ecj:JW3877; -.
DR KEGG; eco:b3906; -.
DR PATRIC; fig|511145.12.peg.4022; -.
DR EchoBASE; EB0835; -.
DR eggNOG; COG1917; Bacteria.
DR eggNOG; COG4977; Bacteria.
DR HOGENOM; CLU_000445_88_5_6; -.
DR InParanoid; P09378; -.
DR OMA; NREVGMT; -.
DR PhylomeDB; P09378; -.
DR BioCyc; EcoCyc:PD00222; -.
DR PRO; PR:P09378; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0019299; P:rhamnose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_01533; HTH_type_RhaR; 1.
DR InterPro; IPR003313; AraC-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR023699; Tscrpt_act_RhaR.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR Pfam; PF02311; AraC_binding; 1.
DR Pfam; PF12833; HTH_18; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Reference proteome; Repeat;
KW Rhamnose metabolism; Transcription; Transcription regulation.
FT CHAIN 1..282
FT /note="HTH-type transcriptional activator RhaR"
FT /id="PRO_0000194551"
FT DOMAIN 179..277
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
FT DNA_BIND 196..217
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
FT DNA_BIND 244..267
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
FT SITE 246
FT /note="Interaction with sigma-70"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01533"
SQ SEQUENCE 282 AA; 32373 MW; 5563D7B0773CEC9D CRC64;
MAHQLKLLKD DFFASDQQAV AVADRYPQDV FAEHTHDFCE LVIVWRGNGL HVLNDRPYRI
TRGDLFYIHA DDKHSYASVN DLVLQNIIYC PERLKLNLDW QGAIPGFNAS AGQPHWRLGS
MGMAQARQVI GQLEHESSQH VPFANEMAEL LFGQLVMLLN RHRYTSDSLP PTSSETLLDK
LITRLAASLK SPFALDKFCD EASCSERVLR QQFRQQTGMT INQYLRQVRV CHAQYLLQHS
RLLISDISTE CGFEDSNYFS VVFTRETGMT PSQWRHLNSQ KD
