RHAS_ECOLI
ID RHAS_ECOLI Reviewed; 278 AA.
AC P09377; Q2M8K2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 186.
DE RecName: Full=HTH-type transcriptional activator RhaS {ECO:0000255|HAMAP-Rule:MF_01534};
DE AltName: Full=L-rhamnose operon regulatory protein RhaS {ECO:0000255|HAMAP-Rule:MF_01534};
GN Name=rhaS {ECO:0000255|HAMAP-Rule:MF_01534}; Synonyms=rhaC2;
GN OrderedLocusNames=b3905, JW3876;
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 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 [6]
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 [7]
RP DNA-BINDING, AND MUTAGENESIS OF LEU-201; ARG-202; HIS-205; ARG-206;
RP CYS-246; GLY-247; PHE-248; SER-249; ASP-250; SER-251; ASN-252; HIS-253;
RP PHE-254; SER-255 AND THR-256.
RC STRAIN=ECL116;
RX PubMed=10464186; DOI=10.1128/jb.181.17.5185-5192.1999;
RA Bhende P.M., Egan S.M.;
RT "Amino acid-DNA contacts by RhaS: an AraC family transcription activator.";
RL J. Bacteriol. 181:5185-5192(1999).
RN [8]
RP INTERACTION WITH SIGMA-70.
RC STRAIN=ECL116;
RX PubMed=10940041; DOI=10.1128/jb.182.17.4959-4969.2000;
RA Bhende P.M., Egan S.M.;
RT "Genetic evidence that transcription activation by RhaS involves specific
RT amino acid contacts with sigma 70.";
RL J. Bacteriol. 182:4959-4969(2000).
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 rhaBAD and rhaT operons.
CC {ECO:0000255|HAMAP-Rule:MF_01534, ECO:0000269|PubMed:8230210,
CC ECO:0000269|PubMed:8757746}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000255|HAMAP-Rule:MF_01534,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01534}.
CC -!- INDUCTION: Induced by RhaR in response to L-rhamnose. Binding of the
CC cAMP receptor protein (CRP) is required for full expression.
CC {ECO:0000269|PubMed:8230210}.
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DR EMBL; X06058; CAA29452.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03038.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76887.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77404.1; -; Genomic_DNA.
DR PIR; S40849; S40849.
DR RefSeq; NP_418341.1; NC_000913.3.
DR RefSeq; WP_000217137.1; NZ_SSZK01000014.1.
DR AlphaFoldDB; P09377; -.
DR SMR; P09377; -.
DR BioGRID; 4260998; 4.
DR BioGRID; 852694; 5.
DR DIP; DIP-10694N; -.
DR IntAct; P09377; 24.
DR STRING; 511145.b3905; -.
DR PaxDb; P09377; -.
DR PRIDE; P09377; -.
DR EnsemblBacteria; AAC76887; AAC76887; b3905.
DR EnsemblBacteria; BAE77404; BAE77404; BAE77404.
DR GeneID; 948397; -.
DR KEGG; ecj:JW3876; -.
DR KEGG; eco:b3905; -.
DR PATRIC; fig|1411691.4.peg.2800; -.
DR EchoBASE; EB0836; -.
DR eggNOG; COG4977; Bacteria.
DR HOGENOM; CLU_000445_88_5_6; -.
DR InParanoid; P09377; -.
DR OMA; GHYPSHW; -.
DR PhylomeDB; P09377; -.
DR BioCyc; EcoCyc:PD00221; -.
DR PRO; PR:P09377; -.
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; IMP:EcoCyc.
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:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0019299; P:rhamnose metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_01534; HTH_type_RhaS; 1.
DR InterPro; IPR003313; AraC-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR037923; HTH-like.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR InterPro; IPR023609; Tscrpt_reg_HTH_RhaS.
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; SSF51215; SSF51215; 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..278
FT /note="HTH-type transcriptional activator RhaS"
FT /id="PRO_0000194563"
FT DOMAIN 174..272
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT DNA_BIND 191..212
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT DNA_BIND 239..262
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT SITE 241
FT /note="Interaction with sigma-70"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT SITE 250
FT /note="Interaction with sigma-70"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01534"
FT MUTAGEN 201
FT /note="L->A: 48% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 202
FT /note="R->A: 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 205
FT /note="H->A: 28% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 206
FT /note="R->A: 0.1% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 246
FT /note="C->A: 66% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 247
FT /note="G->A: 6.2% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 247
FT /note="G->R: 0.9% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 248
FT /note="F->A: 0.9% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 248
FT /note="F->V: 3.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 249
FT /note="S->G: 93% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 250
FT /note="D->A: 8.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 251
FT /note="S->G: 87% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 252
FT /note="N->A: 31% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 252
FT /note="N->H: 0.4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 252
FT /note="N->I: 0.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 252
FT /note="N->S: 37% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 253
FT /note="H->A: 48% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 253
FT /note="H->Q: 32% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 254
FT /note="F->A: 1.2% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 255
FT /note="S->A: 80% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
FT MUTAGEN 256
FT /note="T->A: 61% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:10464186"
SQ SEQUENCE 278 AA; 32315 MW; 64264514484C0D2A CRC64;
MTVLHSVDFF PSGNASVAIE PRLPQADFPE HHHDFHEIVI VEHGTGIHVF NGQPYTITGG
TVCFVRDHDR HLYEHTDNLC LTNVLYRSPD RFQFLAGLNQ LLPQELDGQY PSHWRVNHSV
LQQVRQLVAQ MEQQEGENDL PSTASREILF MQLLLLLRKS SLQENLENSA SRLNLLLAWL
EDHFADEVNW DAVADQFSLS LRTLHRQLKQ QTGLTPQRYL NRLRLMKARH LLRHSEASVT
DIAYRCGFSD SNHFSTLFRR EFNWSPRDIR QGRDGFLQ
