ACNR_CORJK
ID ACNR_CORJK Reviewed; 189 AA.
AC Q4JVM3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=HTH-type transcriptional repressor AcnR {ECO:0000250|UniProtKB:Q8NQ97};
GN Name=acnR {ECO:0000250|UniProtKB:Q8NQ97}; OrderedLocusNames=jk0970;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37134.1; -; Genomic_DNA.
DR RefSeq; WP_011273550.1; NC_007164.1.
DR AlphaFoldDB; Q4JVM3; -.
DR SMR; Q4JVM3; -.
DR STRING; 306537.jk0970; -.
DR EnsemblBacteria; CAI37134; CAI37134; jk0970.
DR KEGG; cjk:jk0970; -.
DR PATRIC; fig|306537.10.peg.981; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_069356_15_12_11; -.
DR OMA; PEFSRGW; -.
DR OrthoDB; 2047542at2; -.
DR Proteomes; UP000000545; 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..189
FT /note="HTH-type transcriptional repressor AcnR"
FT /id="PRO_0000070572"
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 189 AA; 21248 MW; C2D6F6A705F077BA CRC64;
MPKVSDTDLA ERKVEILSGA RHCFATYGYD GATVARLEET IGKSRGAIFH HYGNKDQLFL
EVAHEDMRKM AELAADEGLI GAIRTLVKSN DLTDWWGMRV EITRRVNIDP CFAAKWELDQ
LALRETVRTR LREQRASGRI RKDVEIETIA QTLELVLEGV LGRLAQRQGT EGLSDALDFV
ESALRSPGH
