ID B1J7V9_PSEPW Unreviewed; 144 AA.
AC B1J7V9;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Mercuric resistance operon regulatory protein {ECO:0000256|ARBA:ARBA00017146};
GN OrderedLocusNames=PputW619_2341 {ECO:0000313|EMBL:ACA72841.1};
OS Pseudomonas putida (strain W619).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA72841.1};
RN [1] {ECO:0000313|EMBL:ACA72841.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W619 {ECO:0000313|EMBL:ACA72841.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Psuedomonas putida W619.";
RL Submitted (FEB-2008) 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; CP000949; ACA72841.1; -; Genomic_DNA.
DR AlphaFoldDB; B1J7V9; -.
DR SMR; B1J7V9; -.
DR STRING; 390235.PputW619_2341; -.
DR KEGG; ppw:PputW619_2341; -.
DR eggNOG; COG0789; Bacteria.
DR HOGENOM; CLU_060077_2_0_6; -.
DR OrthoDB; 9808480at2; -.
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; 15763 MW; C573298AFF0846EF CRC64;
MENNLENLTI GVFAKAAGVN VETIRFYQRK GLLLEPDKPY GSIRRYGEAD VTRVRFVKSA
QRLGFSLDEI AELLRLEDGT HCEEASSLAE HKLKDVREKM ADLARMEAVL SELVCACHAR
RGNVSCPLIA SLQGGASLAG SAMP
//
