FNR_VIBCH
ID FNR_VIBCH Reviewed; 250 AA.
AC P0C6D0; Q9KS27;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Fumarate and nitrate reduction regulatory protein;
GN Name=fnr; OrderedLocusNames=VC_1434;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
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DR EMBL; AE003852; AAF94591.1; -; Genomic_DNA.
DR PIR; F82199; F82199.
DR RefSeq; NP_231077.1; NC_002505.1.
DR RefSeq; WP_000622582.1; NZ_LT906614.1.
DR AlphaFoldDB; P0C6D0; -.
DR SMR; P0C6D0; -.
DR STRING; 243277.VC_1434; -.
DR DNASU; 2614066; -.
DR EnsemblBacteria; AAF94591; AAF94591; VC_1434.
DR GeneID; 57740087; -.
DR KEGG; vch:VC_1434; -.
DR PATRIC; fig|243277.26.peg.1364; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_0_2_6; -.
DR OMA; AEVCVMP; -.
DR BioCyc; VCHO:VC1434-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; PF13545; HTH_Crp_2; 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; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..250
FT /note="Fumarate and nitrate reduction regulatory protein"
FT /id="PRO_0000100170"
FT DOMAIN 164..237
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 200..219
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT REGION 23..32
FT /note="Essential for the oxygen-regulated activity"
FT /evidence="ECO:0000250"
FT REGION 50..53
FT /note="Activating region 2A"
FT /evidence="ECO:0000255"
FT REGION 63..64
FT /note="Activating region 3A"
FT /evidence="ECO:0000255"
FT REGION 74..78
FT /note="Activating region 1A"
FT /evidence="ECO:0000255"
FT REGION 84
FT /note="Activating region 3B"
FT /evidence="ECO:0000255"
FT REGION 88..90
FT /note="Activating region 3C"
FT /evidence="ECO:0000255"
FT REGION 115
FT /note="Activating region 3D"
FT /evidence="ECO:0000255"
FT REGION 119..124
FT /note="Activating region 1B"
FT /evidence="ECO:0000255"
FT REGION 126..127
FT /note="Activating region 2B"
FT /evidence="ECO:0000255"
FT REGION 130..131
FT /note="Activating region 2C"
FT /evidence="ECO:0000255"
FT REGION 143..162
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 184..194
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; 28071 MW; A3E3ED036BBBC490 CRC64;
MISEKPAAKR IQSGGCAIHC QDCSISQLCI PFTLNESELD QLDQIIERKK PIQKGQELFK
AGDELRSLYA IRSGTIKSYT ITEQGDEQIT AFHLAGDLVG FDAITGDQHP SFAQALETSM
VCEIPYEILD DLSGKMPKLR QQIMRLMSNE IKGDQEMILL LSKKNAEERL AAFLYNLSTR
FSQRGFSPRE FRLTMTRGDI GNYLGLTVET ISRLLGRFQK SEILSVKGKY ITILNHAELM
ELAGVSKESK
