ID   MERR_PSEAI              Reviewed;         144 AA.
AC   P0A183; P06688;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Mercuric resistance operon regulatory protein;
GN   Name=merR;
OS   Pseudomonas aeruginosa.
OG   Plasmid pVS1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn501;
RX   PubMed=6091128; DOI=10.1073/pnas.81.19.5975;
RA   Misra T.K., Brown N.L., Fritzinger D.C., Pridmore R.D., Barnes W.M.,
RA   Haberstroh L., Silver S.;
RT   "Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the
RT   beginning of the operon including the regulatory region and the first two
RT   structural genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5975-5979(1984).
RN   [2]
RP   MUTAGENESIS.
RX   PubMed=2551364; DOI=10.1021/bi00441a002;
RA   Shewchuk L.M., Verdine G.L., Nash H., Walsh C.T.;
RT   "Mutagenesis of the cysteines in the metalloregulatory protein MerR
RT   indicates that a metal-bridged dimer activates transcription.";
RL   Biochemistry 28:6140-6145(1989).
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.
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; Z00027; CAA77320.1; -; Genomic_DNA.
DR   PIR; A47593; A47593.
DR   RefSeq; WP_003131969.1; NZ_WXZW01000069.1.
DR   PDB; 5CRL; X-ray; 2.80 A; A/B=1-134.
DR   PDBsum; 5CRL; -.
DR   AlphaFoldDB; P0A183; -.
DR   SMR; P0A183; -.
DR   GeneID; 61089172; -.
DR   eggNOG; COG0789; Bacteria.
DR   OMA; CHANGNE; -.
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   InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
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; 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   3D-structure; Activator; DNA-binding; Mercuric resistance; Mercury;
KW   Metal-binding; Plasmid; Repressor; Transcription; Transcription regulation;
KW   Transposable element.
FT   CHAIN           1..144
FT                   /note="Mercuric resistance operon regulatory protein"
FT                   /id="PRO_0000098136"
FT   DOMAIN          7..76
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   DNA_BIND        10..29
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT   BINDING         82
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT   BINDING         117
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT   BINDING         126
FT                   /ligand="Hg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:16793"
FT   MUTAGEN         82
FT                   /note="C->A: Abolishes transcriptional activation."
FT                   /evidence="ECO:0000269|PubMed:2551364"
FT   MUTAGEN         115
FT                   /note="C->A: Slight increase in transcriptional
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:2551364"
FT   MUTAGEN         117
FT                   /note="C->A: Decrease in transcriptional activation."
FT                   /evidence="ECO:0000269|PubMed:2551364"
FT   MUTAGEN         126
FT                   /note="C->S: Abolishes transcriptional activation; loss of
FT                   Hg binding."
FT                   /evidence="ECO:0000269|PubMed:2551364"
FT   HELIX           10..17
FT                   /evidence="ECO:0007829|PDB:5CRL"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:5CRL"
FT   HELIX           48..62
FT                   /evidence="ECO:0007829|PDB:5CRL"
FT   HELIX           67..75
FT                   /evidence="ECO:0007829|PDB:5CRL"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:5CRL"
FT   HELIX           82..118
FT                   /evidence="ECO:0007829|PDB:5CRL"
FT   HELIX           127..132
FT                   /evidence="ECO:0007829|PDB:5CRL"
SQ   SEQUENCE   144 AA;  15763 MW;  C573298AFF0846EF CRC64;
     MENNLENLTI GVFAKAAGVN VETIRFYQRK GLLLEPDKPY GSIRRYGEAD VTRVRFVKSA
     QRLGFSLDEI AELLRLEDGT HCEEASSLAE HKLKDVREKM ADLARMEAVL SELVCACHAR
     RGNVSCPLIA SLQGGASLAG SAMP