ID   ARSR2_PSEPK             Reviewed;         115 AA.
AC   Q88JD1;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Arsenic resistance transcriptional regulator ArsR2 {ECO:0000305};
GN   Name=arsR2 {ECO:0000303|PubMed:27208139};
GN   Synonyms=arsR-II {ECO:0000312|EMBL:AAN68326.1};
GN   OrderedLocusNames=PP_2718 {ECO:0000312|EMBL:AAN68326.1};
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
RN   [2]
RP   FUNCTION, DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=27208139; DOI=10.1128/aem.00606-16;
RA   Fernandez M., Morel B., Ramos J.L., Krell T.;
RT   "Paralogous regulators ArsR1 and ArsR2 of Pseudomonas putida KT2440 as a
RT   basis for arsenic biosensor development.";
RL   Appl. Environ. Microbiol. 82:4133-4144(2016).
CC   -!- FUNCTION: Binds arsenite and regulates the expression of arsenic efflux
CC       pumps. In vitro, also binds antimony and bismuth, but not arsenate.
CC       {ECO:0000269|PubMed:27208139}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27208139}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27208139}.
CC   -!- BIOTECHNOLOGY: Could be used to construct robust and highly sensitive
CC       arsenic biosensors. {ECO:0000269|PubMed:27208139}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE015451; AAN68326.1; -; Genomic_DNA.
DR   RefSeq; NP_744862.1; NC_002947.4.
DR   RefSeq; WP_010953634.1; NC_002947.4.
DR   AlphaFoldDB; Q88JD1; -.
DR   SMR; Q88JD1; -.
DR   STRING; 160488.PP_2718; -.
DR   EnsemblBacteria; AAN68326; AAN68326; PP_2718.
DR   KEGG; ppu:PP_2718; -.
DR   PATRIC; fig|160488.4.peg.2882; -.
DR   eggNOG; COG0640; Bacteria.
DR   HOGENOM; CLU_097806_3_1_6; -.
DR   OMA; CQLVDMF; -.
DR   PhylomeDB; Q88JD1; -.
DR   BioCyc; PPUT160488:G1G01-2899-MON; -.
DR   Proteomes; UP000000556; 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:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
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   Arsenical resistance; Cytoplasm; DNA-binding; Metal-binding;
KW   Metal-thiolate cluster; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..115
FT                   /note="Arsenic resistance transcriptional regulator ArsR2"
FT                   /id="PRO_0000438513"
FT   DOMAIN          1..90
FT                   /note="HTH arsR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   DNA_BIND        31..54
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         30
FT                   /ligand="arsenite"
FT                   /ligand_id="ChEBI:CHEBI:29242"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340,
FT                   ECO:0000305"
FT   BINDING         32
FT                   /ligand="arsenite"
FT                   /ligand_id="ChEBI:CHEBI:29242"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340,
FT                   ECO:0000305"
SQ   SEQUENCE   115 AA;  13113 MW;  B66F9603771FC6C6 CRC64;
     MITPPDVFKS LSDETRARAT LLIASLGELC VCELMCALND SQPKISRHLA QLRSNGMLLD
     RRQGQWVYYR LNPELPSWVH EMLQVTLQAN SQWLADNALR LKNMDGRPVR DSVCC