HMRR_SINMW
ID HMRR_SINMW Reviewed; 147 AA.
AC Q9X5X4; A6UJ52;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=HTH-type transcriptional regulator HmrR;
DE AltName: Full=Copper efflux regulator;
DE AltName: Full=Copper export regulator;
GN Name=hmrR; OrderedLocusNames=Smed_4898;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG Plasmid pSMED01.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS TRANSCRIPTIONAL
RP REGULATOR.
RX PubMed=11936079; DOI=10.1046/j.1365-2958.2002.02791.x;
RA Reeve W.G., Tiwari R.P., Kale N.B., Dilworth M.J., Glenn A.R.;
RT "ActP controls copper homeostasis in Rhizobium leguminosarum bv. viciae and
RT Sinorhizobium meliloti preventing low pH-induced copper toxicity.";
RL Mol. Microbiol. 43:981-991(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the transcription of actP. It detects cytoplasmic
CC copper stress and activates transcription in response to increasing
CC copper concentrations. In the absence of copper, it negatively
CC regulates the transcription of actP. {ECO:0000269|PubMed:11936079}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; AF129004; AAD27640.1; -; Genomic_DNA.
DR EMBL; CP000739; ABR63682.1; -; Genomic_DNA.
DR RefSeq; WP_012061812.1; NC_009620.1.
DR RefSeq; YP_001313615.1; NC_009620.1.
DR AlphaFoldDB; Q9X5X4; -.
DR SMR; Q9X5X4; -.
DR PRIDE; Q9X5X4; -.
DR EnsemblBacteria; ABR63682; ABR63682; Smed_4898.
DR KEGG; smd:Smed_4898; -.
DR PATRIC; fig|366394.8.peg.1376; -.
DR HOGENOM; CLU_060077_2_0_5; -.
DR OMA; FNDPERH; -.
DR OrthoDB; 1661714at2; -.
DR Proteomes; UP000001108; Plasmid pSMED01.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01108; HTH_CueR; 1.
DR InterPro; IPR011789; CueR.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
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; TIGR02044; CueR; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW Activator; Copper; Cytoplasm; DNA-binding; Plasmid; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..147
FT /note="HTH-type transcriptional regulator HmrR"
FT /id="PRO_0000098126"
FT DOMAIN 1..69
FT /note="HTH merR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT DNA_BIND 4..23
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
SQ SEQUENCE 147 AA; 16282 MW; B5DD780622E70AF5 CRC64;
MNIGEASKVS GVSSKMIRYY EQIGLISPAV RTASSYRTYG DNDVHTLRFI RRARDLGFSV
EQIKELLALW RDRSRASSDV KAVALEHIAE LERKIAAIQD MTRTLKHLAS HCHGDGRPDC
PIIEEMAKGG GAAKTEINPR FGVASLK