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Database: UniProt
Entry: A0A5C7EYW1_9PROT
LinkDB: A0A5C7EYW1_9PROT
Original site: A0A5C7EYW1_9PROT 
ID   A0A5C7EYW1_9PROT        Unreviewed;       149 AA.
AC   A0A5C7EYW1;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   RecName: Full=Mercuric resistance operon regulatory protein {ECO:0000256|ARBA:ARBA00017146};
GN   Name=merR {ECO:0000313|EMBL:TXF12282.1};
GN   ORFNames=FR698_07095 {ECO:0000313|EMBL:TXF12282.1};
OS   Pelomicrobium methylotrophicum.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Hydrogenophilia;
OC   Hydrogenophilia incertae sedis; Pelomicrobium.
OX   NCBI_TaxID=2602750 {ECO:0000313|EMBL:TXF12282.1, ECO:0000313|Proteomes:UP000321201};
RN   [1] {ECO:0000313|EMBL:TXF12282.1, ECO:0000313|Proteomes:UP000321201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM250 {ECO:0000313|EMBL:TXF12282.1,
RC   ECO:0000313|Proteomes:UP000321201};
RA   Slobodkina G.B., Merkel A.Y., Slobodkin A.I.;
RT   "Pelomicrobium methylotrophicum gen. nov., sp. nov. a moderately
RT   thermophilic, facultatively anaerobic, lithoautotrophic and methylotrophic
RT   bacterium isolated from a terrestrial mud volcano.";
RL   Submitted (AUG-2019) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TXF12282.1}.
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DR   EMBL; VPFL01000007; TXF12282.1; -; Genomic_DNA.
DR   RefSeq; WP_147799481.1; NZ_VPFL01000007.1.
DR   AlphaFoldDB; A0A5C7EYW1; -.
DR   InParanoid; A0A5C7EYW1; -.
DR   OrthoDB; 5297305at2; -.
DR   Proteomes; UP000321201; Unassembled WGS sequence.
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:SF69; MERR-FAMILY TRANSCRIPTIONAL REGULATOR; 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; PS50937; HTH_MERR_2; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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   Reference proteome {ECO:0000313|Proteomes:UP000321201};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          12..81
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50937"
FT   COILED          91..118
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   149 AA;  16745 MW;  A23B2322238D20A7 CRC64;
     MDTTRIIRQA QALTIGQVAR AAGVNVETIR FYQRRKLMDK PEKPLRGVRR YGRAAVDRVR
     FIKRAQQLGF TLEEVRGLLA LQDGRSCGEA RRLAAAKLES VEERIADLQR MRRVLKTLIG
     QCDTRRGQVA CPIISTLSGV VNAEARLGE
//
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