CSOR_MYCTU
ID CSOR_MYCTU Reviewed; 119 AA.
AC P9WP49; A7Y0H9; F2GHV9; P71543; Q7D919;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Copper-sensing transcriptional repressor CsoR;
DE AltName: Full=Copper-sensitive operon repressor;
GN Name=csoR; Synonyms=croR; OrderedLocusNames=Rv0967;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu T., Ramesh A., Zhang L., George G.N., Talaat A.M., Sacchettini J.C.,
RA Giedroc D.P.;
RT "A novel family of Cu-specific metal sensing transcriptional regulators: M.
RT tuberculosis CpvR.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16586367; DOI=10.1086/502631;
RA Jain S.K., Paul-Satyaseela M., Lamichhane G., Kim K.S., Bishai W.R.;
RT "Mycobacterium tuberculosis invasion and traversal across an in vitro human
RT blood-brain barrier as a pathogenic mechanism for central nervous system
RT tuberculosis.";
RL J. Infect. Dis. 193:1287-1295(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH COPPER ION,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-15; TYR-35; CYS-36; ARG-52;
RP HIS-61 AND GLU-81.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17143269; DOI=10.1038/nchembio844;
RA Liu T., Ramesh A., Ma Z., Ward S.K., Zhang L., George G.N., Talaat A.M.,
RA Sacchettini J.C., Giedroc D.P.;
RT "CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional
RT regulator.";
RL Nat. Chem. Biol. 3:60-68(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 {ECO:0000269|PubMed:17143269}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17143269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Highly up-regulated during the early stages of invasion of
CC the human blood-brain barrier. {ECO:0000269|PubMed:16586367}.
CC -!- DOMAIN: This protein has an antiparallel four-helix bundle architecture
CC that represents a novel DNA-binding fold.
CC -!- SIMILARITY: Belongs to the CsoR family. {ECO:0000305}.
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DR EMBL; DQ778958; ABG82022.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43716.1; -; Genomic_DNA.
DR PIR; E70718; E70718.
DR RefSeq; NP_215482.1; NC_000962.3.
DR RefSeq; WP_003404935.1; NZ_NVQJ01000001.1.
DR PDB; 2HH7; X-ray; 2.55 A; A=1-119.
DR PDBsum; 2HH7; -.
DR AlphaFoldDB; P9WP49; -.
DR SMR; P9WP49; -.
DR STRING; 83332.Rv0967; -.
DR PaxDb; P9WP49; -.
DR DNASU; 885312; -.
DR GeneID; 885312; -.
DR KEGG; mtu:Rv0967; -.
DR TubercuList; Rv0967; -.
DR eggNOG; COG1937; Bacteria.
DR OMA; HLCMPED; -.
DR PhylomeDB; P9WP49; -.
DR Proteomes; UP000001584; Chromosome.
DR CollecTF; EXPREG_00000c70; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0032993; C:protein-DNA complex; EXP:CollecTF.
DR GO; GO:0005507; F:copper ion binding; IDA:MTBBASE.
DR GO; GO:0097077; F:copper ion sensor activity; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; EXP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; EXP:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0046688; P:response to copper ion; IDA:MTBBASE.
DR GO; GO:0010272; P:response to silver ion; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Copper; Cytoplasm; DNA-binding; Metal-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..119
FT /note="Copper-sensing transcriptional repressor CsoR"
FT /id="PRO_0000295581"
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:0000269|PubMed:17143269"
FT BINDING 61
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:17143269"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 15
FT /note="R->A: Loss of ability to bind to DNA; when
FT associated with A-36 and A-52."
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 35
FT /note="Y->F: No effect in ability to bind copper."
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 36
FT /note="C->A: Loss of ability to bind copper; loss of
FT ability to dissociate from DNA in the presence of copper."
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 36
FT /note="C->A: Loss of ability to bind to DNA; when
FT associated with A-15 and A-52."
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 52
FT /note="R->A: Loss of ability to bind to DNA; when
FT associated with A-15 and A-36."
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 61
FT /note="H->A: Loss of ability to bind copper; loss of
FT ability to dissociate from DNA in the presence of copper."
FT /evidence="ECO:0000269|PubMed:17143269"
FT MUTAGEN 81
FT /note="E->A: Decrease in ability to dissociate from DNA in
FT the presence of copper."
FT /evidence="ECO:0000269|PubMed:17143269"
FT HELIX 7..31
FT /evidence="ECO:0007829|PDB:2HH7"
FT HELIX 36..63
FT /evidence="ECO:0007829|PDB:2HH7"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:2HH7"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:2HH7"
SQ SEQUENCE 119 AA; 12800 MW; 87C758FDE4467719 CRC64;
MSKELTAKKR AALNRLKTVR GHLDGIVRML ESDAYCVDVM KQISAVQSSL ERANRVMLHN
HLETCFSTAV LDGHGQAAIE ELIDAVKFTP ALTGPHARLG GAAVGESATE EPMPDASNM
