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Database: UniProt
Entry: Q2L017_BORA1
LinkDB: Q2L017_BORA1
Original site: Q2L017_BORA1 
ID   Q2L017_BORA1            Unreviewed;       131 AA.
AC   Q2L017;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=MerR-family transcriptional regulator {ECO:0000313|EMBL:CAJ49584.1};
GN   OrderedLocusNames=BAV1975 {ECO:0000313|EMBL:CAJ49584.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49584.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ49584.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ49584.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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DR   EMBL; AM167904; CAJ49584.1; -; Genomic_DNA.
DR   RefSeq; WP_012417641.1; NC_010645.1.
DR   AlphaFoldDB; Q2L017; -.
DR   STRING; 360910.BAV1975; -.
DR   GeneID; 41393815; -.
DR   KEGG; bav:BAV1975; -.
DR   eggNOG; COG0789; Bacteria.
DR   HOGENOM; CLU_060077_2_0_4; -.
DR   OrthoDB; 9808480at2; -.
DR   Proteomes; UP000001977; Chromosome.
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 DNA-templated transcription; IEA:InterPro.
DR   CDD; cd01108; HTH_CueR; 1.
DR   Gene3D; 1.10.1660.10; -; 1.
DR   InterPro; IPR011789; CueR.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
DR   InterPro; IPR047057; MerR_fam.
DR   InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
DR   NCBIfam; TIGR02044; CueR; 1.
DR   PANTHER; PTHR30204:SF73; HEAVY METAL-DEPENDENT TRANSCRIPTIONAL REGULATOR HI_0293-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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT   DOMAIN          1..69
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50937"
FT   COILED          81..108
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   131 AA;  14796 MW;  CBC2F7B35EAB142E CRC64;
     MNIGEAARAS GISAKMIRYY ESIGLIHAVS RSEAGYRRYG EDDLHTLQFI RRARNLGFSV
     EQMQELLALW RDRSRASADV KRIALQHVAE LERKADELRE MADTLKHLAR HCHGDGRPDC
     PIIAGLSQLP A
//
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