FNR_ECOL6
ID FNR_ECOL6 Reviewed; 250 AA.
AC P0A9E6; P03019;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Fumarate and nitrate reduction regulatory protein;
GN Name=fnr; OrderedLocusNames=c1807;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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=AAN80271.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN80271.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000611911.1; NC_004431.1.
DR AlphaFoldDB; P0A9E6; -.
DR SMR; P0A9E6; -.
DR STRING; 199310.c1807; -.
DR EnsemblBacteria; AAN80271; AAN80271; c1807.
DR GeneID; 66674838; -.
DR KEGG; ecc:c1807; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_0_2_6; -.
DR OMA; AEVCVMP; -.
DR Proteomes; UP000001410; 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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
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 Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00325; Crp; 1.
DR PRINTS; PR00034; HTHCRP.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 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_0000100162"
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
