CSOR_BACSU
ID CSOR_BACSU Reviewed; 101 AA.
AC O32222;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Copper-sensing transcriptional repressor CsoR;
DE AltName: Full=Copper-sensitive operon repressor;
GN Name=csoR; Synonyms=yvgZ; OrderedLocusNames=BSU33520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION AS A COPZA REGULATOR, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / CU1065;
RX PubMed=18048925; DOI=10.1099/mic.0.2007/011742-0;
RA Smaldone G.T., Helmann J.D.;
RT "CsoR regulates the copper efflux operon copZA in Bacillus subtilis.";
RL Microbiology 153:4123-4128(2007).
RN [3]
RP SUBUNIT, DNA-BINDING, REGULATION BY COPPER, AND MUTAGENESIS OF GLU-90.
RC STRAIN=168 / CU1065;
RX PubMed=19249860; DOI=10.1021/bi900115w;
RA Ma Z., Cowart D.M., Scott R.A., Giedroc D.P.;
RT "Molecular insights into the metal selectivity of the copper(I)-sensing
RT repressor csoR from Bacillus subtilis.";
RL Biochemistry 48:3325-3334(2009).
RN [4]
RP FUNCTION AS YCNJ REGULATOR.
RC STRAIN=ATCC 21332 / IAM 1213;
RX PubMed=19168619; DOI=10.1128/jb.01616-08;
RA Chillappagari S., Miethke M., Trip H., Kuipers O.P., Marahiel M.A.;
RT "Copper acquisition is mediated by ycnJ and regulated by ycnK and csoR in
RT Bacillus subtilis.";
RL J. Bacteriol. 191:2362-2370(2009).
CC -!- FUNCTION: Copper-sensitive repressor that has a key role in copper
CC homeostasis. Negatively regulates expression of the copZA operon and of
CC ycnJ. In the absence of copper ions, binds with high affinity to the
CC copZA promoter and represses the transcription. In the presence of
CC copper ions, CsoR binds Cu(1+), which significantly decreases its DNA
CC binding affinity and leads to the transcription of the genes.
CC {ECO:0000269|PubMed:18048925, ECO:0000269|PubMed:19168619}.
CC -!- SUBUNIT: Homotetramer. Binds DNA with a stoichiometry of 2 tetramers
CC per DNA. {ECO:0000269|PubMed:19249860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a slightly
CC enhanced ability to grow into medium containing high levels of copper.
CC {ECO:0000269|PubMed:18048925}.
CC -!- MISCELLANEOUS: Can also bind other divalent metal ions (zinc, cobalt
CC and nickel), but these metals are poor regulators of DNA binding.
CC -!- SIMILARITY: Belongs to the CsoR family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15357.1; -; Genomic_DNA.
DR PIR; G70041; G70041.
DR RefSeq; NP_391232.1; NC_000964.3.
DR RefSeq; WP_003228404.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32222; -.
DR SMR; O32222; -.
DR STRING; 224308.BSU33520; -.
DR PaxDb; O32222; -.
DR PRIDE; O32222; -.
DR DNASU; 936038; -.
DR EnsemblBacteria; CAB15357; CAB15357; BSU_33520.
DR GeneID; 936038; -.
DR KEGG; bsu:BSU33520; -.
DR PATRIC; fig|224308.179.peg.3637; -.
DR eggNOG; COG1937; Bacteria.
DR InParanoid; O32222; -.
DR OMA; EHLTECI; -.
DR PhylomeDB; O32222; -.
DR BioCyc; BSUB:BSU33520-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
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 Copper; Cytoplasm; DNA-binding; Metal-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..101
FT /note="Copper-sensing transcriptional repressor CsoR"
FT /id="PRO_0000377725"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
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 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT MUTAGEN 90
FT /note="E->A: Abolishes negative regulation of DNA binding,
FT without significantly interfering with the Cu(1+) affinity
FT or coordination geometry."
FT /evidence="ECO:0000269|PubMed:19249860"
SQ SEQUENCE 101 AA; 11475 MW; 925881E4977DBED0 CRC64;
MEKHNEHKTL NHKSSKEKDQ ITNRLKRIEG QVRGIQNMVE NDRYCVDILV QISAVQAAMK
NVALHLLEDH AHHCVADAIK SGDGEQAISE LLDVFKKFTK S
