ACNR_CORGL
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 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=Cgl1541, cg1738;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC 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 / NCIMB
RC 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 / NCIMB
RC 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 / NCIMB
RC 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}.
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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; 58309266; -.
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 OMA; PEFSRGW; -.
DR Proteomes; UP000000582; 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 transcription, DNA-templated; IMP: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 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
