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MERR_STAAU
ID   MERR_STAAU              Reviewed;         135 AA.
AC   P22874;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Mercuric resistance operon regulatory protein;
GN   Name=merR;
OS   Staphylococcus aureus.
OG   Plasmid pI258.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3037534; DOI=10.1073/pnas.84.15.5106;
RA   Laddaga R.A., Chu L., Misra T.K., Silver S.;
RT   "Nucleotide sequence and expression of the mercurial-resistance operon from
RT   Staphylococcus aureus plasmid pI258.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5106-5110(1987).
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   -!- SUBUNIT: Homodimer.
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DR   EMBL; L29436; AAA98241.1; -; Genomic_DNA.
DR   PIR; A29504; A29504.
DR   RefSeq; WP_000525462.1; NZ_WWCF01000007.1.
DR   RefSeq; YP_006937597.1; NC_013319.1.
DR   RefSeq; YP_006937784.1; NC_013323.1.
DR   RefSeq; YP_006938299.1; NC_013337.1.
DR   RefSeq; YP_006938632.1; NC_013347.1.
DR   RefSeq; YP_006938794.1; NC_013352.1.
DR   AlphaFoldDB; P22874; -.
DR   SMR; P22874; -.
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   4: Predicted;
KW   Activator; DNA-binding; Mercuric resistance; Mercury; Metal-binding;
KW   Plasmid; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..135
FT                   /note="Mercuric resistance operon regulatory protein"
FT                   /id="PRO_0000098142"
FT   DOMAIN          1..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"
SQ   SEQUENCE   135 AA;  15741 MW;  FDC1A852621D4F82 CRC64;
     MGMKISELAK ACDVNKETVR YYERKGLIAG PPRNESGYRI YSEETADRVR FIKRMKELDF
     SLKEIHLLFG VVDQDGERCK DMYAFTVQKT KEIERKVQGL LRIQRLLEEL KEKCPDEKAM
     YTCPIIETLM GGPDK
 
 
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