ID SOXR_ECO57 Reviewed; 154 AA.
AC P0ACS3; P22538; Q53442;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Redox-sensitive transcriptional activator SoxR;
GN Name=soxR; OrderedLocusNames=Z5662, ECs5045;
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE005174; AAG59261.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38468.1; -; Genomic_DNA.
DR PIR; A86100; A86100.
DR PIR; E91259; E91259.
DR RefSeq; NP_313072.1; NC_002695.1.
DR RefSeq; WP_000412428.1; NZ_VOAI01000008.1.
DR AlphaFoldDB; P0ACS3; -.
DR SMR; P0ACS3; -.
DR STRING; 155864.Z5662; -.
DR GeneID; 83579088; -.
DR GeneID; 914292; -.
DR KEGG; ece:Z5662; -.
DR KEGG; ecs:ECs_5045; -.
DR PATRIC; fig|386585.9.peg.5268; -.
DR eggNOG; COG0789; Bacteria.
DR HOGENOM; CLU_060077_5_1_6; -.
DR OMA; SCPLRNP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd01110; HTH_SoxR; 1.
DR Gene3D; 1.10.1660.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR047057; MerR_fam.
DR InterPro; IPR010211; Redox-sen_tscrpt-act_SoxR.
DR InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
DR NCBIfam; TIGR01950; SoxR; 1.
DR PANTHER; PTHR30204; REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR; 1.
DR PANTHER; PTHR30204:SF0; REDOX-SENSITIVE TRANSCRIPTIONAL ACTIVATOR SOXR; 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; Putative DNA-binding domain; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Activator; DNA-binding; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..154
FT /note="Redox-sensitive transcriptional activator SoxR"
FT /id="PRO_0000098151"
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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 17150 MW; 9A715120860EEC9B CRC64;
MEKKLPRIKA LLTPGEVAKR SGVAVSALHF YESKGLITSI RNSGNQRRYK RDVLRYVAII
KIAQRIGIPL ATIGEAFGVL PEGHTLSAKE WKQLSSQWRE ELDRRIHTLV ALRDELDGCI
GCGCLSRSDC PLRNPGDRLG EEGTGARLLE DEQN
//
