RBSR_ECOL6
ID RBSR_ECOL6 Reviewed; 330 AA.
AC P0ACQ1; P25551;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ribose operon repressor;
GN Name=rbsR; OrderedLocusNames=c4681;
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: Transcriptional repressor for the ribose rbsDACBK operon.
CC RbsR binds to a region of perfect dyad symmetry spanning the rbs operon
CC transcriptional start site. The affinity for the rbs operator is
CC reduced by addition of ribose, consistent with ribose being the inducer
CC of the operon (By similarity). {ECO:0000250}.
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DR EMBL; AE014075; AAN83113.1; -; Genomic_DNA.
DR RefSeq; WP_000224470.1; NC_004431.1.
DR AlphaFoldDB; P0ACQ1; -.
DR SMR; P0ACQ1; -.
DR STRING; 199310.c4681; -.
DR EnsemblBacteria; AAN83113; AAN83113; c4681.
DR GeneID; 58463882; -.
DR KEGG; ecc:c4681; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR OMA; IMQRYPS; -.
DR BioCyc; ECOL199310:C4681-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR046335; LacI/GalR-like_sensor.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..330
FT /note="Ribose operon repressor"
FT /id="PRO_0000107987"
FT DOMAIN 2..56
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 4..23
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ SEQUENCE 330 AA; 36612 MW; AA651205A4109CAE CRC64;
MATMKDVARL AGVSTSTVSH VINKDRFVSE AITAKVEAAI KELNYAPSAL ARSLKLNQTH
TIGMLITAST NPFYSELVRG VERSCFERGY SLVLCNTEGD EQRMNRNLET LMQKRVDGLL
LLCTETHQPS REIMQRYPTV PTVMMDWAPF DGDSDLIQDN SLLGGDLATQ YLIDKGHTRI
ACITGPLDKT PARLRLEGYR AAMKRAGLNI PDGYEVTGDF EFNGGFDAMR QLLSHPLRPQ
AVFTGNDAMA VGVYQALYQA ELQVPQDIAV IGYDDIELAS FMTPPLTTIH QPKDELGELA
IDVLIHRITQ PTLQQQRLQL TPILMERGSA