ID   FNR_SALTI               Reviewed;         250 AA.
AC   Q8Z787;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Fumarate and nitrate reduction regulatory protein;
GN   Name=fnr; OrderedLocusNames=STY1404, t1564;
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(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   -!- SEQUENCE CAUTION:
CC       Sequence=AAO69195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAD01670.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL513382; CAD01670.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014613; AAO69195.1; ALT_INIT; Genomic_DNA.
DR   PIR; AE0662; AE0662.
DR   RefSeq; NP_455844.3; NC_003198.1.
DR   RefSeq; WP_000611917.1; NZ_WSUR01000041.1.
DR   AlphaFoldDB; Q8Z787; -.
DR   SMR; Q8Z787; -.
DR   STRING; 220341.gene:17585360; -.
DR   KEGG; stt:t1564; -.
DR   KEGG; sty:STY1404; -.
DR   PATRIC; fig|220341.7.peg.1414; -.
DR   eggNOG; COG0664; Bacteria.
DR   HOGENOM; CLU_075053_0_2_6; -.
DR   OMA; IFMEGEP; -.
DR   OrthoDB; 7643467at2; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..250
FT                   /note="Fumarate and nitrate reduction regulatory protein"
FT                   /id="PRO_0000100166"
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;  27882 MW;  05EBCFA29727CD2C CRC64;
     MIPEKRIIRR IQSGGCAIHC QDCSISQLCI PFTLNEHELD QLDNIIERKK PIQKGQTLFK
     AGDELKSLYA IRSGTIKSYT ITEQGDEQIT GFHLAGDLVG FDAIGSGHHP SFAQALETSM
     VCKIPFETLD DLSGKMPNLR QQMMRLMSGE IKGDQDMILL LSKKNAEERL AAFIYNLSRR
     FAQRGFSPRE FRLTMTRGDI GNYLGLTVET ISRLLGRFQK SGMLAVKGKY ITIENSDALA
     ALAGHTRNVA
//