ID ACNR_CORGL Reviewed; 188 AA. AC Q8NQ97; Q6M549; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=HTH-type transcriptional repressor AcnR {ECO:0000303|PubMed:15494411}; DE AltName: Full=TetR-type regulator AcnR {ECO:0000303|PubMed:15494411}; GN Name=acnR {ECO:0000303|PubMed:15494411}; GN OrderedLocusNames=Cgl1541, cg1738; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). RN [3] RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=15494411; DOI=10.1074/jbc.m408271200; RA Krug A., Wendisch V.F., Bott M.; RT "Identification of AcnR, a TetR-type repressor of the aconitase gene acn in RT Corynebacterium glutamicum."; RL J. Biol. Chem. 280:585-595(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-188 IN COMPLEX WITH CITRATE AND RP MAGNESIUM, FUNCTION, MUTAGENESIS OF LYS-43; LYS-55; GLU-65; ASP-66; ARG-99; RP LYS-104; ARG-141 AND ASP-143, AND SUBUNIT. RX PubMed=23589369; DOI=10.1074/jbc.m113.462440; RA Garcia-Nafria J., Baumgart M., Turkenburg J.P., Wilkinson A.J., Bott M., RA Wilson K.S.; RT "Crystal and solution studies reveal that the transcriptional regulator RT AcnR of Corynebacterium glutamicum is regulated by citrate-Mg2+ binding to RT a non-canonical pocket."; RL J. Biol. Chem. 288:15800-15812(2013). CC -!- FUNCTION: AcnR negatively controls the expression of the aconitase gene CC acn. Binds to the imperfect inverted repeat in the acn promoter region. CC {ECO:0000269|PubMed:15494411, ECO:0000269|PubMed:23589369}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15494411, CC ECO:0000269|PubMed:23589369}. CC -!- DISRUPTION PHENOTYPE: Deletion of acnR leads to a 5-fold increase of CC the aconitase activity. Overexpression of acnR leads to a 2-fold CC decrease of the aconitase activity. {ECO:0000269|PubMed:15494411}. 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; BA000036; BAB98934.1; -; Genomic_DNA. DR EMBL; BX927152; CAF21549.1; -; Genomic_DNA. DR RefSeq; NP_600756.1; NC_003450.3. DR RefSeq; WP_003856101.1; NC_006958.1. DR PDB; 4AC6; X-ray; 2.54 A; A=2-188. DR PDB; 4ACI; X-ray; 1.65 A; A/B=2-188. DR PDB; 4AF5; X-ray; 1.90 A; A=1-188. DR PDBsum; 4AC6; -. DR PDBsum; 4ACI; -. DR PDBsum; 4AF5; -. DR AlphaFoldDB; Q8NQ97; -. DR SMR; Q8NQ97; -. DR STRING; 196627.cg1738; -. DR GeneID; 69622052; -. DR KEGG; cgb:cg1738; -. DR KEGG; cgl:Cgl1541; -. DR PATRIC; fig|196627.13.peg.1508; -. DR eggNOG; COG1309; Bacteria. DR HOGENOM; CLU_069356_15_12_11; -. DR OrthoDB; 5816932at2; -. DR BioCyc; CORYNE:G18NG-11126-MONOMER; -. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; Chromosome. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf. DR PANTHER; PTHR30055; HTH-TYPE TRANSCRIPTIONAL REGULATOR RUTR; 1. DR PANTHER; PTHR30055:SF226; HTH-TYPE TRANSCRIPTIONAL REPRESSOR RV1474C; 1. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR SUPFAM; SSF48498; Tetracyclin repressor-like, C-terminal domain; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Magnesium; Metal-binding; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1..188 FT /note="HTH-type transcriptional repressor AcnR" FT /id="PRO_0000070571" 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:0000269|PubMed:23589369" FT BINDING 130 FT /ligand="citrate" FT /ligand_id="ChEBI:CHEBI:16947" FT /evidence="ECO:0000269|PubMed:23589369" FT BINDING 134 FT /ligand="citrate" FT /ligand_id="ChEBI:CHEBI:16947" FT /evidence="ECO:0000269|PubMed:23589369" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:23589369" FT BINDING 185 FT /ligand="citrate" FT /ligand_id="ChEBI:CHEBI:16947" FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 43 FT /note="K->A: DNA binding affinity is almost completely FT abolished. Still forms a dimer." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 55 FT /note="K->A: DNA binding affinity is almost completely FT abolished. Still forms a dimer but the ratio of aggregated FT to dimeric protein is significantly higher." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 65 FT /note="E->A: No effect on DNA binding." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 66 FT /note="D->A: No effect on DNA binding." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 99 FT /note="R->A: Weaker binding to DNA." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 104 FT /note="K->A: DNA binding affinity is slightly reduced. FT Still forms a dimer but the ratio of aggregated to dimeric FT protein is significantly higher." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 109 FT /note="D->A: No effect on DNA binding." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 141 FT /note="R->A: No effect on DNA binding." FT /evidence="ECO:0000269|PubMed:23589369" FT MUTAGEN 143 FT /note="D->A: No effect on DNA binding." FT /evidence="ECO:0000269|PubMed:23589369" FT HELIX 12..31 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 34..41 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 45..52 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 55..88 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 93..101 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 103..108 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 110..119 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 121..136 FT /evidence="ECO:0007829|PDB:4ACI" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 146..165 FT /evidence="ECO:0007829|PDB:4ACI" FT HELIX 173..184 FT /evidence="ECO:0007829|PDB:4ACI" SQ SEQUENCE 188 AA; 21185 MW; 54F31FA9A184B836 CRC64; MSVAAGDKPT NSRQEILEGA RRCFAEHGYE GATVRRLEEA TGKSRGAIFH HFGDKENLFL ALAREDAARM AEVVSENGLV EVMRGMLEDP ERYDWMSVRL EISKQLRTDP VFRAKWIDHQ SVLDEAVRVR LSRNVDKGQM RTDVPIEVLH TFLETVLDGF ISRLATGAST EGLSEVLDLV EGTVRKRD //