ACNR_COREF
ID ACNR_COREF Reviewed; 188 AA.
AC Q8FTA6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, 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=CE1663;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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; BA000035; BAC18473.1; -; Genomic_DNA.
DR RefSeq; WP_006767665.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FTA6; -.
DR SMR; Q8FTA6; -.
DR STRING; 196164.23493503; -.
DR EnsemblBacteria; BAC18473; BAC18473; BAC18473.
DR KEGG; cef:CE1663; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_069356_15_12_11; -.
DR OMA; PEFSRGW; -.
DR OrthoDB; 2047542at2; -.
DR Proteomes; UP000001409; 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..188
FT /note="HTH-type transcriptional repressor AcnR"
FT /id="PRO_0000070570"
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 188 AA; 21272 MW; EA2D4BEC5F3A645E CRC64;
MSVATGDKPV NSRQEILEGA RRCFAEHGYE GATVRRLEEA TGKSRGAIFH HFGDKEKLFL
ALAREDAARM AETVSENGLV EVMRGMLEDP ERYDWLSIRL EISKQLRTDP EFRAKWTDHQ
SVLDEAVRVR LARNADKGRM RTDVPIEVLH LYLETVMDGF ISRLATGAST EGLSEVLDLV
ETSVRRPD
