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 27-MAR-2024, entry version 135.
DE RecName: Full=HTH-type transcriptional repressor AseR;
GN Name=aseR; Synonyms=ydeT; OrderedLocusNames=BSU05330;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; 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; 224308-BSU05330; -.
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 OrthoDB; 9798835at2; -.
DR PhylomeDB; P96677; -.
DR BioCyc; BSUB:BSU05330-MONOMER; -.
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 DNA-templated transcription; IBA:GO_Central.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; NF033788; HTH_metalloreg; 1.
DR PANTHER; PTHR33154:SF18; ARSENICAL RESISTANCE OPERON REPRESSOR; 1.
DR PANTHER; PTHR33154; TRANSCRIPTIONAL REGULATOR, ARSR FAMILY; 1.
DR Pfam; PF01022; HTH_5; 1.
DR PRINTS; PR00778; HTHARSR.
DR SMART; SM00418; HTH_ARSR; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
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