ID   ASER_BACSU              Reviewed;         111 AA.
AC   P96677; Q797H3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=HTH-type transcriptional repressor AseR;
GN   Name=aseR; Synonyms=ydeT; OrderedLocusNames=BSU05330;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF CYS-33 AND CYS-35.
RC   STRAIN=168;
RX   PubMed=16430705; DOI=10.1111/j.1365-2958.2006.05029.x;
RA   Harvie D.R., Andreini C., Cavallaro G., Meng W., Connolly B.A., Yoshida K.,
RA   Fujita Y., Harwood C.R., Radford D.S., Tottey S., Cavet J.S.,
RA   Robinson N.J.;
RT   "Predicting metals sensed by ArsR-SmtB repressors: allosteric interference
RT   by a non-effector metal.";
RL   Mol. Microbiol. 59:1341-1356(2006).
CC   -!- FUNCTION: Metal-responsive transcriptional regulator that represses
CC       transcription of the aseR-ydfA operon by binding specifically to its
CC       promoter. Binding of arsenite or antimonite causes the repressor to
CC       dissociate from the DNA. {ECO:0000269|PubMed:16430705}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Can also bind zinc in vitro, but it does not impair DNA
CC       binding.
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DR   EMBL; AB001488; BAA19367.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12340.1; -; Genomic_DNA.
DR   PIR; F69779; F69779.
DR   RefSeq; NP_388414.1; NC_000964.3.
DR   RefSeq; WP_003243257.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P96677; -.
DR   SMR; P96677; -.
DR   STRING; 224308.BSU05330; -.
DR   PaxDb; P96677; -.
DR   PRIDE; P96677; -.
DR   EnsemblBacteria; CAB12340; CAB12340; BSU_05330.
DR   GeneID; 938089; -.
DR   KEGG; bsu:BSU05330; -.
DR   PATRIC; fig|224308.179.peg.569; -.
DR   eggNOG; COG0640; Bacteria.
DR   InParanoid; P96677; -.
DR   OMA; CQLVDMF; -.
DR   PhylomeDB; P96677; -.
DR   BioCyc; BSUB:BSU05330-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01022; HTH_5; 1.
DR   PRINTS; PR00778; HTHARSR.
DR   SMART; SM00418; HTH_ARSR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50987; HTH_ARSR_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Metal-binding; Metal-thiolate cluster;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..111
FT                   /note="HTH-type transcriptional repressor AseR"
FT                   /id="PRO_0000378471"
FT   DOMAIN          1..105
FT                   /note="HTH arsR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   DNA_BIND        34..57
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         33
FT                   /ligand="arsenite"
FT                   /ligand_id="ChEBI:CHEBI:29242"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         35
FT                   /ligand="arsenite"
FT                   /ligand_id="ChEBI:CHEBI:29242"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         39
FT                   /ligand="arsenite"
FT                   /ligand_id="ChEBI:CHEBI:29242"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   MUTAGEN         33
FT                   /note="C->S: Binds DNA, but loss of arsenite-mediated
FT                   regulation; when associated with S-35."
FT                   /evidence="ECO:0000269|PubMed:16430705"
FT   MUTAGEN         35
FT                   /note="C->S: Binds DNA, but loss of arsenite-mediated
FT                   regulation; when associated with S-33."
FT                   /evidence="ECO:0000269|PubMed:16430705"
SQ   SEQUENCE   111 AA;  13088 MW;  3E2B4088061AB1A3 CRC64;
     MTIDVAAMTR CLKTLSDQTR LIMMRLFLEQ EYCVCQLVDM FEMSQPAISQ HLRKLKNAGF
     VNEDRRGQWR YYSINGSCPE FDTLQLILHQ IDQEDELLNH IKQKKTQACC Q