ID   CSOR_MYCBP              Reviewed;         119 AA.
AC   A1KHA2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Copper-sensing transcriptional repressor CsoR;
DE   AltName: Full=Copper-sensitive operon repressor;
GN   Name=csoR; OrderedLocusNames=BCG_1021;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC   -!- FUNCTION: Copper-sensitive repressor that has a key role in copper
CC       homeostasis. It is part of the cso operon involved in the cellular
CC       response to increasing concentrations of copper inside the bacterium,
CC       which can be highly toxic. In the presence of copper, CsoR fully
CC       dissociates from the promoter in the cso operon, leading to the
CC       transcription of its genes. Binds to a GC-rich pseudopallindromic
CC       sequence, 5'-GTAGCCCACCCCCAGTGGGGTGGGA-3', in the cso promoter region
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: This protein has an antiparallel four-helix bundle architecture
CC       that represents a novel DNA-binding fold. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CsoR family. {ECO:0000305}.
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DR   EMBL; AM408590; CAL71008.1; -; Genomic_DNA.
DR   RefSeq; WP_003404935.1; NC_008769.1.
DR   AlphaFoldDB; A1KHA2; -.
DR   SMR; A1KHA2; -.
DR   KEGG; mbb:BCG_1021; -.
DR   HOGENOM; CLU_130332_1_1_11; -.
DR   OMA; HLCMPED; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProt.
DR   Gene3D; 1.20.58.1000; -; 1.
DR   InterPro; IPR003735; Metal_Tscrpt_repr.
DR   InterPro; IPR038390; Metal_Tscrpt_repr_sf.
DR   PANTHER; PTHR33677; PTHR33677; 1.
DR   Pfam; PF02583; Trns_repr_metal; 1.
PE   3: Inferred from homology;
KW   Copper; Cytoplasm; DNA-binding; Metal-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..119
FT                   /note="Copper-sensing transcriptional repressor CsoR"
FT                   /id="PRO_0000295580"
FT   REGION          99..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   119 AA;  12800 MW;  87C758FDE4467719 CRC64;
     MSKELTAKKR AALNRLKTVR GHLDGIVRML ESDAYCVDVM KQISAVQSSL ERANRVMLHN
     HLETCFSTAV LDGHGQAAIE ELIDAVKFTP ALTGPHARLG GAAVGESATE EPMPDASNM