ID Q44190_ALCFA Unreviewed; 144 AA.
AC Q44190;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Mercuric resistance operon regulatory protein {ECO:0000256|ARBA:ARBA00017146};
GN Name=merR {ECO:0000313|EMBL:CAA83892.1};
OS Alcaligenes faecalis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=511 {ECO:0000313|EMBL:CAA83892.1};
RN [1] {ECO:0000313|EMBL:CAA83892.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SE20 {ECO:0000313|EMBL:CAA83892.1};
RA Osborn A.M., Bruce K.D., Strike P., Ritchie D.A.;
RT "Sequence Conservation between Regulatory Mercury Resistance Genes from
RT Mercury Polluted and Pristine Environments.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; Z33484; CAA83892.1; -; Genomic_DNA.
DR PIR; S51706; S51706.
DR AlphaFoldDB; Q44190; -.
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 NCBIfam; TIGR02051; MerR; 1.
DR PANTHER; PTHR30204:SF67; HTH-TYPE TRANSCRIPTIONAL REGULATOR MLRA-RELATED; 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; PS00552; HTH_MERR_1; 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 7..76
FT /note="HTH merR-type"
FT /evidence="ECO:0000259|PROSITE:PS50937"
SQ SEQUENCE 144 AA; 15832 MW; B71D7FF3C980DC49 CRC64;
MENNLENLTI GVFAKAAGVN VETIRFYQRK GLLPEPDKPY GSIRRYGEAD VVRVKFVKSA
QRLGFSLDEI AELLRLDDGT HCEEASSLAE HKLKDVREKM ADLARMETVL SELVCACHAR
KGNVSCPLIA SLQGEGGLAR SAMP
//