SOXR_ECOLI
ID SOXR_ECOLI Reviewed; 154 AA.
AC P0ACS2; P22538; Q2M6P1; Q53442;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Redox-sensitive transcriptional activator SoxR;
GN Name=soxR; Synonyms=marC; OrderedLocusNames=b4063, JW4024;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1708380; DOI=10.1128/jb.173.9.2864-2871.1991;
RA Wu J., Weiss B.;
RT "Two divergently transcribed genes, soxR and soxS, control a superoxide
RT response regulon of Escherichia coli.";
RL J. Bacteriol. 173:2864-2871(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1653416; DOI=10.1093/nar/19.16.4479;
RA Amabile-Cuevas C.F., Demple B.;
RT "Molecular characterization of the soxRS genes of Escherichia coli: two
RT genes control a superoxide stress regulon.";
RL Nucleic Acids Res. 19:4479-4484(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(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 IRON-SULFUR.
RX PubMed=8306957; DOI=10.1002/j.1460-2075.1994.tb06243.x;
RA Hidalgo E., Demple B.;
RT "An iron-sulfur center essential for transcriptional activation by the
RT redox-sensing SoxR protein.";
RL EMBO J. 13:138-146(1994).
RN [7]
RP EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX PubMed=7673113; DOI=10.1074/jbc.270.36.20908;
RA Hidalgo E., Bollinger J.M. Jr., Bradley T.M., Walsh C.T., Demple B.;
RT "Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role
RT of the metal centers in transcription.";
RL J. Biol. Chem. 270:20908-20914(1995).
RN [8]
RP REDOX TITRATION.
RX PubMed=8969171; DOI=10.1074/jbc.271.52.33173;
RA Ding H., Hidalgo E., Demple B.;
RT "The redox state of the [2Fe-2S] clusters in SoxR protein regulates its
RT activity as a transcription factor.";
RL J. Biol. Chem. 271:33173-33175(1996).
RN [9]
RP IRON-SULFUR CLUSTER ASSEMBLY, AND EPR SPECTROSCOPY.
RX PubMed=8631739; DOI=10.1074/jbc.271.13.7269;
RA Hidalgo E., Demple B.;
RT "Activation of SoxR-dependent transcription in vitro by noncatalytic or
RT NifS-mediated assembly of [2Fe-2S] clusters into apo-SoxR.";
RL J. Biol. Chem. 271:7269-7272(1996).
RN [10]
RP MUTAGENESIS, EPR SPECTROSCOPY, AND REDOX TITRATION.
RX PubMed=9019397; DOI=10.1016/s0092-8674(00)81864-4;
RA Hidalgo E., Ding H., Demple B.;
RT "Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR
RT sensor-regulator to the oxidized form.";
RL Cell 88:121-129(1997).
RN [11]
RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY.
RX PubMed=9092651; DOI=10.1093/nar/25.8.1469;
RA Bradley T.M., Hidalgo E., Leautaud V., Ding H., Demple B.;
RT "Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and
RT the role of the [2Fe-2S] centers in transcriptional activation.";
RL Nucleic Acids Res. 25:1469-1475(1997).
RN [12]
RP REVIEW.
RX PubMed=9204707; DOI=10.1016/s0968-0004(97)01068-2;
RA Hidalgo E., Ding H., Demple B.;
RT "Redox signal transduction via iron-sulfur clusters in the SoxR
RT transcription activator.";
RL Trends Biochem. Sci. 22:207-210(1997).
RN [13]
RP REVIEW.
RX PubMed=10207625;
RA Demple B., Hidalgo E., Ding H.;
RT "Transcriptional regulation via redox-sensitive iron-sulphur centres in an
RT oxidative stress response.";
RL Biochem. Soc. Symp. 64:119-128(1999).
RN [14]
RP MUTAGENESIS.
RX PubMed=12670967; DOI=10.1128/jb.185.8.2441-2450.2003;
RA Chander M., Raducha-Grace L., Demple B.;
RT "Transcription-defective soxR mutants of Escherichia coli: isolation and in
RT vivo characterization.";
RL J. Bacteriol. 185:2441-2450(2003).
RN [15]
RP VARIANT SOXR102 CYS-20.
RX PubMed=8065907; DOI=10.1093/nar/22.15.2958;
RA Nunoshiba T., Demple B.;
RT "A cluster of constitutive mutations affecting the C-terminus of the redox-
RT sensitive SoxR transcriptional activator.";
RL Nucleic Acids Res. 22:2958-2962(1994).
CC -!- FUNCTION: Activates the transcription of the soxS gene which itself
CC controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-
CC sulfur cluster that may act as a redox sensor system that recognizes
CC superoxide. The variable redox state of the Fe-S cluster is employed in
CC vivo to modulate the transcriptional activity of SoxR in response to
CC specific types of oxidative stress. Upon reduction of 2Fe-2S cluster,
CC SoxR reversibly loses its transcriptional activity, but retains its DNA
CC binding affinity.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -285 mV.;
CC -!- SUBUNIT: Homodimer.
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DR EMBL; M60111; AAA24641.1; -; Genomic_DNA.
DR EMBL; X59593; CAA42162.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43157.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77033.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78065.1; -; Genomic_DNA.
DR EMBL; S72675; AAB31680.1; -; Genomic_DNA.
DR PIR; JS0577; JS0577.
DR RefSeq; NP_418487.1; NC_000913.3.
DR RefSeq; WP_000412428.1; NZ_STEB01000014.1.
DR PDB; 2ZHG; X-ray; 2.80 A; A=1-154.
DR PDB; 2ZHH; X-ray; 3.20 A; A=1-154.
DR PDBsum; 2ZHG; -.
DR PDBsum; 2ZHH; -.
DR AlphaFoldDB; P0ACS2; -.
DR SMR; P0ACS2; -.
DR BioGRID; 4259601; 10.
DR BioGRID; 852860; 1.
DR DIP; DIP-29848N; -.
DR IntAct; P0ACS2; 7.
DR STRING; 511145.b4063; -.
DR PaxDb; P0ACS2; -.
DR PRIDE; P0ACS2; -.
DR EnsemblBacteria; AAC77033; AAC77033; b4063.
DR EnsemblBacteria; BAE78065; BAE78065; BAE78065.
DR GeneID; 67414700; -.
DR GeneID; 948566; -.
DR KEGG; ecj:JW4024; -.
DR KEGG; eco:b4063; -.
DR PATRIC; fig|1411691.4.peg.2642; -.
DR EchoBASE; EB0950; -.
DR eggNOG; COG0789; Bacteria.
DR HOGENOM; CLU_060077_5_1_6; -.
DR InParanoid; P0ACS2; -.
DR OMA; IHFYEAK; -.
DR PhylomeDB; P0ACS2; -.
DR BioCyc; EcoCyc:PD04132; -.
DR EvolutionaryTrace; P0ACS2; -.
DR PRO; PR:P0ACS2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR CDD; cd01110; HTH_SoxR; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR010211; Redox-sen_tscrpt-act_SoxR.
DR InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
DR PANTHER; PTHR30204:SF0; PTHR30204:SF0; 1.
DR Pfam; PF00376; MerR; 1.
DR Pfam; PF09278; MerR-DNA-bind; 1.
DR PRINTS; PR00040; HTHMERR.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR01950; SoxR; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Activator; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..154
FT /note="Redox-sensitive transcriptional activator SoxR"
FT /id="PRO_0000098150"
FT DOMAIN 11..79
FT /note="HTH merR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT DNA_BIND 14..33
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT REGION 119..130
FT /note="Might be part of a sensor region"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 122
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 124
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 130
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT VARIANT 20
FT /note="R -> C (in soxR102; constitutively activated
FT allele)"
FT /evidence="ECO:0000269|PubMed:8065907"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:2ZHG"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:2ZHG"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2ZHH"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2ZHG"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2ZHG"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:2ZHG"
FT HELIX 88..119
FT /evidence="ECO:0007829|PDB:2ZHG"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2ZHG"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2ZHG"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2ZHG"
SQ SEQUENCE 154 AA; 17150 MW; 9A715120860EEC9B CRC64;
MEKKLPRIKA LLTPGEVAKR SGVAVSALHF YESKGLITSI RNSGNQRRYK RDVLRYVAII
KIAQRIGIPL ATIGEAFGVL PEGHTLSAKE WKQLSSQWRE ELDRRIHTLV ALRDELDGCI
GCGCLSRSDC PLRNPGDRLG EEGTGARLLE DEQN
