ID   MODE_SHIFL              Reviewed;         262 AA.
AC   P0A9H0; P46930;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Transcriptional regulator ModE;
GN   Name=modE; OrderedLocusNames=SF0543, S0551;
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: The ModE-Mo complex acts as a repressor of the modABC operon,
CC       involved in the transport of molybdate. Upon binding molybdate, the
CC       conformation of the protein changes, promoting dimerization of ModE-Mo.
CC       The protein dimer is then competent to bind a DNA region, upstream of
CC       the modABC operon. Acts also as an enhancer of the expression of genes
CC       coding for molybdoenzymes, both directly and indirectly (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ModE family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN42187.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16060.1; -; Genomic_DNA.
DR   RefSeq; NP_706480.1; NC_004337.2.
DR   RefSeq; WP_001147439.1; NZ_WPGW01000046.1.
DR   AlphaFoldDB; P0A9H0; -.
DR   SMR; P0A9H0; -.
DR   STRING; 198214.SF0543; -.
DR   EnsemblBacteria; AAN42187; AAN42187; SF0543.
DR   EnsemblBacteria; AAP16060; AAP16060; S0551.
DR   GeneID; 1023462; -.
DR   GeneID; 66670968; -.
DR   KEGG; sfl:SF0543; -.
DR   KEGG; sfx:S0551; -.
DR   PATRIC; fig|198214.7.peg.632; -.
DR   HOGENOM; CLU_087839_0_0_6; -.
DR   OMA; SYKTAWH; -.
DR   OrthoDB; 1582630at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0015689; P:molybdate ion transport; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR016462; ModE.
DR   InterPro; IPR003725; ModE-bd_N.
DR   InterPro; IPR004606; Mop_domain.
DR   InterPro; IPR005116; Transp-assoc_OB_typ1.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03459; TOBE; 2.
DR   PIRSF; PIRSF005763; Txn_reg_ModE; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF50331; SSF50331; 2.
DR   TIGRFAMs; TIGR00637; ModE_repress; 1.
DR   TIGRFAMs; TIGR00638; Mop; 1.
DR   PROSITE; PS51866; MOP; 2.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Molybdenum; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Transport.
FT   CHAIN           1..262
FT                   /note="Transcriptional regulator ModE"
FT                   /id="PRO_0000201128"
FT   DOMAIN          124..191
FT                   /note="Mop 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   DOMAIN          196..260
FT                   /note="Mop 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01213"
FT   DNA_BIND        33..79
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          1..121
FT                   /note="I"
FT   REGION          125..133
FT                   /note="Required for dimer formation and molybdate binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  28281 MW;  9A17636162F4233E CRC64;
     MQAEILLTLK LQQKLFADPR RISLLKHIAL SGSISQGAKD AGISYKSAWD AINEMNQLSE
     HILVERATGG KGGGGAVLTR YGQRLIQLYD LLAQIQQKAF DVLSDDDALP LNSLLAAISR
     FSLQTSARNQ WFGTITARDH DDVQQHVDVL LADGKTRLKV AITAQSGARL GLDEGKEVLI
     LLKAPWVGIT QDEAVAQNAD NQLPGIISHI ERGAEQCEVL MALPDGQTLC ATVPVNEATS
     LQQGQNVTAY FNADSVIIAT LC