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Database: UniProt
Entry: H1SH44_9BURK
LinkDB: H1SH44_9BURK
Original site: H1SH44_9BURK 
ID   H1SH44_9BURK            Unreviewed;       133 AA.
AC   H1SH44;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Mercuric resistance operon regulatory protein {ECO:0000256|ARBA:ARBA00017146};
GN   ORFNames=OR16_38724 {ECO:0000313|EMBL:EHP38157.1};
OS   Cupriavidus basilensis OR16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP38157.1, ECO:0000313|Proteomes:UP000005808};
RN   [1] {ECO:0000313|EMBL:EHP38157.1, ECO:0000313|Proteomes:UP000005808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR16 {ECO:0000313|EMBL:EHP38157.1,
RC   ECO:0000313|Proteomes:UP000005808};
RX   PubMed=22461549; DOI=10.1128/JB.06752-11;
RA   Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA   Nagy I., Horvath B., Nagy I., Kukolya J.;
RT   "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL   J. Bacteriol. 194:2109-2110(2012).
CC   -!- FUNCTION: Mediates the mercuric-dependent induction of mercury
CC       resistance operon. In the absence of mercury MerR represses
CC       transcription by binding tightly to the mer operator region; when
CC       mercury is present the dimeric complex binds a single ion and becomes a
CC       potent transcriptional activator, while remaining bound to the mer
CC       site. {ECO:0000256|ARBA:ARBA00024874}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHP38157.1}.
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DR   EMBL; AHJE01000142; EHP38157.1; -; Genomic_DNA.
DR   RefSeq; WP_006163838.1; NZ_AHJE01000142.1.
DR   AlphaFoldDB; H1SH44; -.
DR   PATRIC; fig|1127483.3.peg.7707; -.
DR   OrthoDB; 9808480at2; -.
DR   Proteomes; UP000005808; Unassembled WGS sequence.
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:0045340; F:mercury ion binding; IEA:InterPro.
DR   GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
DR   CDD; cd04783; HTH_MerR1; 1.
DR   Gene3D; 1.10.1660.10; -; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR011794; MerR.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
DR   InterPro; IPR047057; MerR_fam.
DR   InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
DR   PANTHER; PTHR30204:SF87; MULTIDRUG-EFFLUX TRANSPORTER 1 REGULATOR; 1.
DR   PANTHER; PTHR30204; REDOX-CYCLING DRUG-SENSING TRANSCRIPTIONAL ACTIVATOR SOXR; 1.
DR   Pfam; PF00376; MerR; 1.
DR   Pfam; PF09278; MerR-DNA-bind; 1.
DR   PRINTS; PR00040; HTHMERR.
DR   SMART; SM00422; HTH_MERR; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   PROSITE; PS50937; HTH_MERR_2; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Mercuric resistance {ECO:0000256|ARBA:ARBA00022466};
KW   Mercury {ECO:0000256|ARBA:ARBA00022914};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT   DOMAIN          4..73
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50937"
SQ   SEQUENCE   133 AA;  14592 MW;  1BBE1B7E8E9DE523 CRC64;
     MESTLTIGQV AKAANVGVET VRYYHRRGLL PVPERAHGGV RQYSRESLQR LSFIRRAQAL
     GFTLEEIRAL LQLNDGSTCG AARALAEHKL QAVDERLREL QALRTDLHRL IGQCHANGGT
     GSCPLIETLC ASS
//
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