ID   BADR_RHOPA              Reviewed;         175 AA.
AC   O07458;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Transcriptional activatory protein BadR;
DE   AltName: Full=Benzoate anaerobic degradation regulator;
GN   Name=badR; OrderedLocusNames=RPA0655;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=9177244; DOI=10.1073/pnas.94.12.6484;
RA   Egland P.G., Pelletier D.A., Dispensa M., Gibson J., Harwood C.S.;
RT   "A cluster of bacterial genes for anaerobic benzene ring biodegradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:6484-6489(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10094687; DOI=10.1128/jb.181.7.2102-2109.1999;
RA   Egland P.G., Harwood C.S.;
RT   "BadR, a new MarR family member, regulates anaerobic benzoate degradation
RT   by Rhodopseudomonas palustris in concert with AadR, an Fnr family member.";
RL   J. Bacteriol. 181:2102-2109(1999).
CC   -!- FUNCTION: Transcriptional activator of genes for the anaerobic
CC       degradation of benzoate.
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DR   EMBL; U75363; AAC23923.1; -; Genomic_DNA.
DR   EMBL; BX572595; CAE26099.1; -; Genomic_DNA.
DR   PIR; T51765; T51765.
DR   RefSeq; WP_011156222.1; NC_005296.1.
DR   AlphaFoldDB; O07458; -.
DR   SMR; O07458; -.
DR   STRING; 258594.RPA0655; -.
DR   PRIDE; O07458; -.
DR   DNASU; 2692633; -.
DR   EnsemblBacteria; CAE26099; CAE26099; RPA0655.
DR   GeneID; 66891678; -.
DR   KEGG; rpa:RPA0655; -.
DR   eggNOG; COG1846; Bacteria.
DR   HOGENOM; CLU_083287_18_7_5; -.
DR   OMA; RLYQCAN; -.
DR   PhylomeDB; O07458; -.
DR   BioCyc; RPAL258594:TX73_RS03385-MON; -.
DR   Proteomes; UP000001426; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000835; HTH_MarR-typ.
DR   InterPro; IPR023187; Tscrpt_reg_MarR-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF12802; MarR_2; 1.
DR   SMART; SM00347; HTH_MARR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS01117; HTH_MARR_1; 1.
DR   PROSITE; PS50995; HTH_MARR_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..175
FT                   /note="Transcriptional activatory protein BadR"
FT                   /id="PRO_0000054352"
FT   DOMAIN          20..156
FT                   /note="HTH marR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
SQ   SEQUENCE   175 AA;  19519 MW;  6BEC68C23E9B0DC6 CRC64;
     MMAKKRVATD NAADAKMELA NRLFFRLYQC ANMLHKTGTR AVEAEGLTTQ QWAVLGALSR
     PTVANGMSVG DLARYLMVSR QNLTGLIGRM ERDGHVAVVP DERDRRSRLV TMTKSGRHVW
     EVLAQPKIRA YYGEVLGDFS INDVTHTLHY LLKILDNMKR LDDGAAGETA ATDLE