ID   FNR_SHIFL               Reviewed;         250 AA.
AC   P0A9E8; P03019;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Fumarate and nitrate reduction regulatory protein;
GN   Name=fnr; OrderedLocusNames=SF1836, S1434;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; 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: Global transcription factor that controls the expression of
CC       over 100 target genes in response to anoxia. It facilitates the
CC       adaptation to anaerobic growth conditions by regulating the expression
CC       of gene products that are involved in anaerobic energy metabolism. When
CC       the terminal electron acceptor, O(2), is no longer available, it
CC       represses the synthesis of enzymes involved in aerobic respiration and
CC       increases the synthesis of enzymes required for anaerobic respiration
CC       (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005674; AAN43398.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16836.1; -; Genomic_DNA.
DR   RefSeq; NP_707691.2; NC_004337.2.
DR   RefSeq; WP_000611911.1; NZ_WPGW01000191.1.
DR   AlphaFoldDB; P0A9E8; -.
DR   SMR; P0A9E8; -.
DR   STRING; 198214.SF1836; -.
DR   PaxDb; 198214-SF1836; -.
DR   GeneID; 1025042; -.
DR   GeneID; 83576524; -.
DR   KEGG; sfl:SF1836; -.
DR   KEGG; sfx:S1434; -.
DR   PATRIC; fig|198214.7.peg.2184; -.
DR   HOGENOM; CLU_075053_0_2_6; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 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   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00092; HTH_CRP; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR012318; HTH_CRP.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR24567:SF75; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF13545; HTH_Crp_2; 1.
DR   PRINTS; PR00034; HTHCRP.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00419; HTH_CRP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS00042; HTH_CRP_1; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Activator; Cytoplasm; DNA-binding; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..250
FT                   /note="Fumarate and nitrate reduction regulatory protein"
FT                   /id="PRO_0000100169"
FT   DOMAIN          164..237
FT                   /note="HTH crp-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   DNA_BIND        197..216
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   REGION          20..29
FT                   /note="Essential for the oxygen-regulated activity"
FT                   /evidence="ECO:0000250"
FT   REGION          47..50
FT                   /note="Activating region 2A"
FT                   /evidence="ECO:0000255"
FT   REGION          60..61
FT                   /note="Activating region 3A"
FT                   /evidence="ECO:0000255"
FT   REGION          71..75
FT                   /note="Activating region 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          81
FT                   /note="Activating region 3B"
FT                   /evidence="ECO:0000255"
FT   REGION          85..87
FT                   /note="Activating region 3C"
FT                   /evidence="ECO:0000255"
FT   REGION          112
FT                   /note="Activating region 3D"
FT                   /evidence="ECO:0000255"
FT   REGION          116..121
FT                   /note="Activating region 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          123..124
FT                   /note="Activating region 2B"
FT                   /evidence="ECO:0000255"
FT   REGION          127..128
FT                   /note="Activating region 2C"
FT                   /evidence="ECO:0000255"
FT   REGION          140..159
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255"
FT   REGION          181..191
FT                   /note="Activating region 1C"
FT                   /evidence="ECO:0000255"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         23
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         29
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         122
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   250 AA;  27967 MW;  33F7BFA2972FF703 CRC64;
     MIPEKRIIRR IQSGGCAIHC QDCSISQLCI PFTLNEHELD QLDNIIERKK PIQKGQTLFK
     AGDELKSLYA IRSGTIKSYT ITEQGDEQIT GFHLAGDLVG FDAIGSGHHP SFAQALETSM
     VCEIPFETLD DLSGKMPNLR QQMMRLMSGE IKGDQDMILL LSKKNAEERL AAFIYNLSRR
     FAQRGFSPRE FRLTMTRGDI GNYLGLTVET ISRLLGRFQK SGMLAVKGKY ITIENNDALA
     QLAGHTRNVA
//