SOXR_SHIFL
ID SOXR_SHIFL Reviewed; 154 AA.
AC P0ACS4; P22538; Q53442;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Redox-sensitive transcriptional activator SoxR;
GN Name=soxR; OrderedLocusNames=SF4123, S3590;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45547.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18635.1; -; Genomic_DNA.
DR RefSeq; NP_709840.1; NC_004337.2.
DR RefSeq; WP_000412428.1; NZ_WPGW01000153.1.
DR AlphaFoldDB; P0ACS4; -.
DR SMR; P0ACS4; -.
DR STRING; 198214.SF4123; -.
DR EnsemblBacteria; AAN45547; AAN45547; SF4123.
DR EnsemblBacteria; AAP18635; AAP18635; S3590.
DR GeneID; 1026084; -.
DR GeneID; 67414700; -.
DR KEGG; sfl:SF4123; -.
DR KEGG; sfx:S3590; -.
DR PATRIC; fig|198214.7.peg.4862; -.
DR HOGENOM; CLU_060077_5_1_6; -.
DR OMA; IHFYEAK; -.
DR OrthoDB; 1677723at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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: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; IEA:InterPro.
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 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_0000098154"
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
