ACNR_CORDI
ID ACNR_CORDI Reviewed; 190 AA.
AC Q6NH62;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=HTH-type transcriptional repressor AcnR {ECO:0000250|UniProtKB:Q8NQ97};
GN Name=acnR {ECO:0000250|UniProtKB:Q8NQ97}; OrderedLocusNames=DIP1284;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
CC -!- FUNCTION: AcnR negatively controls the expression of the aconitase gene
CC acn. {ECO:0000250|UniProtKB:Q8NQ97}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8NQ97}.
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DR EMBL; BX248357; CAE49811.1; -; Genomic_DNA.
DR RefSeq; WP_010934950.1; NC_002935.2.
DR AlphaFoldDB; Q6NH62; -.
DR SMR; Q6NH62; -.
DR STRING; 257309.DIP1284; -.
DR EnsemblBacteria; CAE49811; CAE49811; DIP1284.
DR GeneID; 29422804; -.
DR KEGG; cdi:DIP1284; -.
DR HOGENOM; CLU_069356_15_12_11; -.
DR OMA; PEFSRGW; -.
DR OrthoDB; 2047542at2; -.
DR Proteomes; UP000002198; Chromosome.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Magnesium; Metal-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..190
FT /note="HTH-type transcriptional repressor AcnR"
FT /id="PRO_0000070569"
FT DOMAIN 10..70
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 33..52
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT BINDING 79..80
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:Q8NQ97"
FT BINDING 130
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:Q8NQ97"
FT BINDING 134
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:Q8NQ97"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NQ97"
FT BINDING 185
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /evidence="ECO:0000250|UniProtKB:Q8NQ97"
SQ SEQUENCE 190 AA; 21831 MW; 849460E6FAB4E6CE CRC64;
MPVVSNTELS MRRQEILEGA RRCFAEHGYE GATVRRLEET VGKSRGAIFH HFSDKENLFL
ALAREDAARM AEVVAENGLV EVMRDMLAHP ERHDWLATRL EITKMLRTDP SFRNRWIEHQ
RVLDDAVLER LQRNAHLGRM RDDVPIDVLH TYLETVLDGF ISRLASGGDT DNLERVLDLV
EESVRSSQPS