ID   AADR_RHOPA              Reviewed;         239 AA.
AC   Q01980;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Transcriptional activatory protein AadR;
DE   AltName: Full=Anaerobic aromatic degradation regulator;
GN   Name=aadR; OrderedLocusNames=RPA4234;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=1522059; DOI=10.1128/jb.174.18.5803-5813.1992;
RA   Dispensa M., Thomas C.T., Kim M.-K., Perrotta J.A., Gibson J.,
RA   Harwood C.S.;
RT   "Anaerobic growth of Rhodopseudomonas palustris on 4-hydroxybenzoate is
RT   dependent on AadR, a member of the cyclic AMP receptor protein family of
RT   transcriptional regulators.";
RL   J. Bacteriol. 174:5803-5813(1992).
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 anaerobic gene expression. For
CC       aromatic acid degradation. Also required for the anaerobic degradation
CC       of benzoate.
CC   -!- MISCELLANEOUS: Possesses 4 cysteines which may bind a metal ion
CC       (possibly iron).
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DR   EMBL; M92426; AAA26090.1; -; Genomic_DNA.
DR   EMBL; BX572606; CAE29675.1; -; Genomic_DNA.
DR   PIR; B43334; B43334.
DR   RefSeq; WP_011159769.1; NZ_CP116810.1.
DR   AlphaFoldDB; Q01980; -.
DR   SMR; Q01980; -.
DR   STRING; 258594.RPA4234; -.
DR   GeneID; 66895360; -.
DR   eggNOG; COG0664; Bacteria.
DR   HOGENOM; CLU_075053_0_1_5; -.
DR   PhylomeDB; Q01980; -.
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   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00092; HTH_CRP; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR012318; HTH_CRP.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR24567:SF75; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00325; Crp; 1.
DR   PRINTS; PR00034; HTHCRP.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00419; HTH_CRP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS00042; HTH_CRP_1; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..239
FT                   /note="Transcriptional activatory protein AadR"
FT                   /id="PRO_0000100141"
FT   DOMAIN          158..231
FT                   /note="HTH crp-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   DNA_BIND        191..210
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT   BINDING         27..149
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   239 AA;  26711 MW;  392ED15225566020 CRC64;
     MPHLAYPTTT CEGFRCETHC AVRGLAICGE LGPADHEEFE RLAQHVRYGP KEALFSEDEV
     ADSVYSLIEG IARLYKLLPD GRRQIIGFAL PGDFLGMAPG NRYSFSADSI GGVTVCKFFR
     GPFLRFIENR PQMLLRMNDF ATRELSLAQD QMLLLGRRSA EEKVAAFLVG WRDRLARLEG
     VTKTVSLPMG RQDIADFLGL TIETVSRTFT KLEREKLIVI VPDGVRVLDP KRFDALAAA
//