RBSR_ECOLI
ID RBSR_ECOLI Reviewed; 330 AA.
AC P0ACQ0; P25551; Q2M871;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Ribose operon repressor;
GN Name=rbsR; OrderedLocusNames=b3753, JW3732;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-7 AND 251-257.
RC STRAIN=K12;
RX PubMed=1304369; DOI=10.1002/pro.5560010701;
RA Mauzy C.A., Hermodson M.A.;
RT "Structural and functional analyses of the repressor, RbsR, of the ribose
RT operon of Escherichia coli.";
RL Protein Sci. 1:831-842(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Iida A., Teshiba S., Mizobuchi K.;
RT "Characterization of rbsR: the repressor gene for ribose operon in
RT Escherichia coli.";
RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
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 [5]
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 [6]
RP SIMILARITY TO RIBOSE-BINDING PROTEINS.
RX PubMed=1304370; DOI=10.1002/pro.5560010702;
RA Mauzy C.A., Hermodson M.A.;
RT "Structural homology between rbs repressor and ribose binding protein
RT implies functional similarity.";
RL Protein Sci. 1:843-849(1992).
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.
CC -!- INTERACTION:
CC P0ACQ0; Q46864: mqsA; NbExp=3; IntAct=EBI-1119646, EBI-1120353;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M13169; AAA51477.1; -; Genomic_DNA.
DR EMBL; D10466; BAA01259.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62106.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76776.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77535.1; -; Genomic_DNA.
DR PIR; B65179; B65179.
DR RefSeq; NP_418209.1; NC_000913.3.
DR RefSeq; WP_000224470.1; NZ_SSZK01000036.1.
DR AlphaFoldDB; P0ACQ0; -.
DR SMR; P0ACQ0; -.
DR BioGRID; 4261326; 10.
DR BioGRID; 852568; 1.
DR IntAct; P0ACQ0; 5.
DR STRING; 511145.b3753; -.
DR PaxDb; P0ACQ0; -.
DR PRIDE; P0ACQ0; -.
DR EnsemblBacteria; AAC76776; AAC76776; b3753.
DR EnsemblBacteria; BAE77535; BAE77535; BAE77535.
DR GeneID; 58463882; -.
DR GeneID; 948266; -.
DR KEGG; ecj:JW3732; -.
DR KEGG; eco:b3753; -.
DR PATRIC; fig|1411691.4.peg.2947; -.
DR EchoBASE; EB0812; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_2_6; -.
DR InParanoid; P0ACQ0; -.
DR OMA; IMQRYPS; -.
DR PhylomeDB; P0ACQ0; -.
DR BioCyc; EcoCyc:PD03867; -.
DR PRO; PR:P0ACQ0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1304369"
FT CHAIN 2..330
FT /note="Ribose operon repressor"
FT /id="PRO_0000107985"
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"
FT CONFLICT 12..13
FT /note="GV -> L (in Ref. 1; AAA51477)"
FT /evidence="ECO:0000305"
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
