MERR_SALTI
ID MERR_SALTI Reviewed; 144 AA.
AC P0A2Q8; P07044;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Mercuric resistance operon regulatory protein;
GN Name=merR; OrderedLocusNames=HCM1.235;
OS Salmonella typhi.
OG Plasmid pHCM1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
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 site
CC (By similarity). {ECO:0000250}.
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DR EMBL; AL513383; CAD09817.1; -; Genomic_DNA.
DR RefSeq; NP_569425.1; NC_003384.1.
DR RefSeq; WP_000429836.1; NZ_WSUR01000067.1.
DR AlphaFoldDB; P0A2Q8; -.
DR SMR; P0A2Q8; -.
DR KEGG; sty:HCM1.235; -.
DR PATRIC; fig|220341.7.peg.5252; -.
DR HOGENOM; CLU_060077_2_0_6; -.
DR OMA; HRTESSY; -.
DR Proteomes; UP000000541; Plasmid pHCM1.
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 3: Inferred from homology;
KW Activator; DNA-binding; Mercuric resistance; Mercury; Metal-binding;
KW Plasmid; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..144
FT /note="Mercuric resistance operon regulatory protein"
FT /id="PRO_0000098139"
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 /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT /evidence="ECO:0000250"
SQ SEQUENCE 144 AA; 15905 MW; 8BEEC928A7B83EE9 CRC64;
MENNLENLTI GVFAKAAGVN VETIRFYQRK GLLREPDKPY GSIRRYGEAD VVRVKFVKSA
QRLGFSLDEI AELLRLDDGT HCEEASSLAE HKLKDVREKM ADLARMETVL SELVCACHAR
KGNVSCPLIA SLQGEAGLAR SAMP