ID   MERR_BACCE              Reviewed;         132 AA.
AC   P22853;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Mercuric resistance operon regulatory protein;
GN   Name=merR1; Synonyms=merR;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RC607; TRANSPOSON=Tn5084;
RX   PubMed=2536669; DOI=10.1128/jb.171.1.83-92.1989;
RA   Wang Y., Moore M., Levinson H.S., Silver S., Walsh C.T., Mahler I.;
RT   "Nucleotide sequence of a chromosomal mercury resistance determinant from a
RT   Bacillus sp. with broad-spectrum mercury resistance.";
RL   J. Bacteriol. 171:83-92(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RC607; TRANSPOSON=Tn5084;
RX   PubMed=10559175; DOI=10.1128/jb.181.22.7080-7086.1999;
RA   Gupta A., Phung L.T., Chakravarty L., Silver S.;
RT   "Mercury resistance in Bacillus cereus RC607: transcriptional organization
RT   and two new open reading frames.";
RL   J. Bacteriol. 181:7080-7086(1999).
RN   [3]
RP   FUNCTION.
RX   PubMed=2492496; DOI=10.1128/jb.171.1.222-229.1989;
RA   Helmann J.D., Wang Y., Mahler I., Walsh C.T.;
RT   "Homologous metalloregulatory proteins from both Gram-positive and Gram-
RT   negative bacteria control transcription of mercury resistance operons.";
RL   J. Bacteriol. 171:222-229(1989).
RN   [4]
RP   MUTAGENESIS.
RX   PubMed=2305262; DOI=10.1126/science.2305262;
RA   Helmann J.D., Ballard B.T., Walsh C.T.;
RT   "The MerR metalloregulatory protein binds mercuric ion as a tricoordinate,
RT   metal-bridged dimer.";
RL   Science 247:946-948(1990).
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:0000269|PubMed:2492496}.
CC   -!- SUBUNIT: Homodimer.
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DR   EMBL; AF138877; AAA83973.1; -; Genomic_DNA.
DR   EMBL; AB066362; BAB62429.1; -; Genomic_DNA.
DR   PIR; A32239; A32239.
DR   RefSeq; WP_000672080.1; NZ_VEGO01000042.1.
DR   AlphaFoldDB; P22853; -.
DR   SMR; P22853; -.
DR   PRIDE; P22853; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045340; F:mercury ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
DR   CDD; cd04783; HTH_MerR1; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR011794; MerR.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
DR   Pfam; PF13411; MerR_1; 1.
DR   PRINTS; PR00040; HTHMERR.
DR   SMART; SM00422; HTH_MERR; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   TIGRFAMs; TIGR02051; MerR; 1.
DR   PROSITE; PS00552; HTH_MERR_1; 1.
DR   PROSITE; PS50937; HTH_MERR_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Mercuric resistance; Mercury; Metal-binding;
KW   Repressor; Transcription; Transcription regulation; Transposable element.
FT   CHAIN           1..132
FT                   /note="Mercuric resistance operon regulatory protein"
FT                   /id="PRO_0000098135"
FT   DOMAIN          2..71
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   DNA_BIND        5..24
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   BINDING         79
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT   BINDING         114
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT   BINDING         123
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT   MUTAGEN         79
FT                   /note="C->A,H: Loss of mercury binding."
FT                   /evidence="ECO:0000269|PubMed:2305262"
FT   MUTAGEN         114
FT                   /note="C->A: Loss of mercury binding."
FT                   /evidence="ECO:0000269|PubMed:2305262"
FT   MUTAGEN         123
FT                   /note="C->A,H: Loss of mercury binding."
FT                   /evidence="ECO:0000269|PubMed:2305262"
SQ   SEQUENCE   132 AA;  15971 MW;  6557FBF1FB95B635 CRC64;
     MKFRIGELAD KCGVNKETIR YYERLGLIPE PERTEKGYRM YSQQTVDRLH FIKRMQELGF
     TLNEIDKLLG VVDRDEAKCR DMYDFTILKI EDIQRKIEDL KRIERMLMDL KERCPENKDI
     YECPIIETLM KK