ID A8AGD2_CITK8 Unreviewed; 276 AA.
AC A8AGD2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Fumarate/nitrate reduction transcriptional regulator {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=CKO_01409 {ECO:0000313|EMBL:ABV12545.1};
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV12545.1, ECO:0000313|Proteomes:UP000008148};
RN [1] {ECO:0000313|EMBL:ABV12545.1, ECO:0000313|Proteomes:UP000008148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC {ECO:0000313|Proteomes:UP000008148};
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|ARBA:ARBA00037339}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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; CP000822; ABV12545.1; -; Genomic_DNA.
DR AlphaFoldDB; A8AGD2; -.
DR STRING; 290338.CKO_01409; -.
DR KEGG; cko:CKO_01409; -.
DR HOGENOM; CLU_075053_0_2_6; -.
DR Proteomes; UP000008148; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008148}.
FT DOMAIN 56..139
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 190..263
FT /note="HTH crp-type"
FT /evidence="ECO:0000259|PROSITE:PS51063"
SQ SEQUENCE 276 AA; 30804 MW; 1FB70F0AC360EF37 CRC64;
MGVAQAYVLT KKMLKLTNIN YGLSRPMIPE KRIIRRIQSG GCAIHCQDCS ISQLCIPFTL
NEHELDQLDN IIERKKPIQK GQTLFKAGDE LKSLYAIRSG TIKSYTITEQ GDEQITGFHL
AGDLVGFDAI GSGHHPSFAQ ALETSMVCEI PFETLDDLSG KMPNLRQQMM RLMSGEIKGD
QDMILLLSKK NAEERLAAFI YNLSRRFAQR GFSPREFRLT MTRGDIGNYL GLTVETISRL
LGRFQKSGML AVKGKYITIE NSDALAVLAG HTRNVA
//
