RHAR_ECOL6
ID RHAR_ECOL6 Reviewed; 282 AA.
AC Q8FBD7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 25-MAY-2022, entry version 113.
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}; OrderedLocusNames=c4856;
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: Activates expression of the rhaSR operon in response to L-
CC rhamnose. {ECO:0000255|HAMAP-Rule:MF_01533}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000255|HAMAP-Rule:MF_01533}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01533}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN83284.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN83284.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001298410.1; NZ_CP051263.1.
DR AlphaFoldDB; Q8FBD7; -.
DR SMR; Q8FBD7; -.
DR STRING; 199310.c4856; -.
DR EnsemblBacteria; AAN83284; AAN83284; c4856.
DR KEGG; ecc:c4856; -.
DR eggNOG; COG1917; Bacteria.
DR eggNOG; COG4977; Bacteria.
DR HOGENOM; CLU_000445_88_5_6; -.
DR Proteomes; UP000001410; 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; IEA:InterPro.
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 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 3: Inferred from homology;
KW Activator; Cytoplasm; DNA-binding; Repeat; Rhamnose metabolism;
KW Transcription; Transcription regulation.
FT CHAIN 1..282
FT /note="HTH-type transcriptional activator RhaR"
FT /id="PRO_0000194552"
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; 32304 MW; EA3E9D564149FB32 CRC64;
MAHQLKLLKD DFFASDQQAV AVADRYPQDV FAEHTHDFCE LVIVWRGNGL HVLNDRPYRI
TRGDLFYIHA DDKHSYASVN DLVLQNIIYC PERLKLNLDW QGAIPGFSAS AGQPHWRLGS
VGMAQARQVI GQLEHESSQH VSFANEMAEL LFGQLVMLLN RHRYTSDSLP PTSSETLLDK
LITRLAASLK SPFALDKFCD EASCSERVLR QQFRQQTGMT INQYLRQVRV CHAQYLLQHS
RLLISDISTE CGFEDSNYFS VVFTRETGMT PSQWRHLNSQ KD