ID F0TD53_9PROT Unreviewed; 144 AA.
AC F0TD53;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Mercuric resistance operon regulatory protein {ECO:0000256|ARBA:ARBA00017146};
GN ORFNames=NAL212_0097 {ECO:0000313|EMBL:ADZ28043.1};
OS Nitrosomonas sp. AL212.
OG Plasmid pNAL21202 {ECO:0000313|EMBL:ADZ28043.1,
OG ECO:0000313|Proteomes:UP000001629}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ28043.1, ECO:0000313|Proteomes:UP000001629};
RN [1] {ECO:0000313|EMBL:ADZ28043.1, ECO:0000313|Proteomes:UP000001629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ28043.1,
RC ECO:0000313|Proteomes:UP000001629};
RC PLASMID=Plasmid pNAL21202 {ECO:0000313|Proteomes:UP000001629};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT "Complete sequence of plasmid2 of Nitrosomonas sp. AL212.";
RL Submitted (FEB-2011) 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; CP002554; ADZ28043.1; -; Genomic_DNA.
DR AlphaFoldDB; F0TD53; -.
DR KEGG; nit:NAL212_0097; -.
DR HOGENOM; CLU_060077_2_0_4; -.
DR Proteomes; UP000001629; Plasmid pNAL21202.
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 Plasmid {ECO:0000313|EMBL:ADZ28043.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001629};
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; 15857 MW; 8FDECD844D0351BE CRC64;
MGNNLENLTI GVFAKVAGVN VETIRFYQRK GLLSEPDKPY GSIRRYGEAD VTRVRFVKSA
QRLGFSLDEI AELLRLEDGT HCEEASSLAE HKLKDVREKM ADLARMEAVL SDLVCACHAR
KGNVSCPLIA SLQGKKEPHS AAVT
//
