ID   POBR_ACIAD              Reviewed;         271 AA.
AC   Q43992;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=p-hydroxybenzoate hydroxylase transcriptional activator;
GN   Name=pobR; OrderedLocusNames=ACIAD1718;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8331077; DOI=10.1128/jb.175.14.4499-4506.1993;
RA   Dimarco A.A., Averhoff B.A., Ornston L.N.;
RT   "Identification of the transcriptional activator pobR and characterization
RT   of its role in the expression of pobA, the structural gene for p-
RT   hydroxybenzoate hydroxylase in Acinetobacter calcoaceticus.";
RL   J. Bacteriol. 175:4499-4506(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Positive regulator of the pobA gene for p-hydroxybenzoate
CC       hydroxylase.
CC   -!- INDUCTION: By p-hydroxybenzoate.
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DR   EMBL; L05770; AAC37162.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68560.1; -; Genomic_DNA.
DR   PIR; A36893; A36893.
DR   RefSeq; WP_004926666.1; NC_005966.1.
DR   PDB; 5HPF; X-ray; 2.31 A; A/B/C=96-271.
DR   PDB; 5HPI; X-ray; 2.96 A; A/B/C/D=96-271.
DR   PDBsum; 5HPF; -.
DR   PDBsum; 5HPI; -.
DR   AlphaFoldDB; Q43992; -.
DR   SMR; Q43992; -.
DR   STRING; 62977.ACIAD1718; -.
DR   EnsemblBacteria; CAG68560; CAG68560; ACIAD1718.
DR   GeneID; 45234105; -.
DR   KEGG; aci:ACIAD1718; -.
DR   eggNOG; COG1414; Bacteria.
DR   HOGENOM; CLU_062618_0_1_6; -.
DR   OMA; LDKRDWI; -.
DR   OrthoDB; 370329at2; -.
DR   BioCyc; ASP62977:ACIAD_RS07920-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046278; P:3,4-dihydroxybenzoate metabolic process; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR012794; PcaR_PcaU.
DR   InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR   InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF09339; HTH_IclR; 1.
DR   Pfam; PF01614; IclR; 1.
DR   SMART; SM00346; HTH_ICLR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   TIGRFAMs; TIGR02431; pcaR_pcaU; 1.
DR   PROSITE; PS51077; HTH_ICLR; 1.
DR   PROSITE; PS51078; ICLR_ED; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Aromatic hydrocarbons catabolism; DNA-binding;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..271
FT                   /note="p-hydroxybenzoate hydroxylase transcriptional
FT                   activator"
FT                   /id="PRO_0000201766"
FT   DOMAIN          23..83
FT                   /note="HTH iclR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   DOMAIN          98..271
FT                   /note="IclR-ED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00394"
FT   DNA_BIND        45..64
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   MUTAGEN         61
FT                   /note="R->H: In ADP249; loss of activity."
FT   HELIX           97..113
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:5HPI"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   HELIX           160..167
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   HELIX           171..181
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   HELIX           194..207
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   STRAND          220..228
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   STRAND          234..243
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   HELIX           249..254
FT                   /evidence="ECO:0007829|PDB:5HPF"
FT   HELIX           256..270
FT                   /evidence="ECO:0007829|PDB:5HPF"
SQ   SEQUENCE   271 AA;  30764 MW;  40B7DA8531389084 CRC64;
     MEQHHQYLAH PHSSEEIRTE DYIAGLAKGL ALLEAFGIDR QRLNVTQVAE RTGISRTAAR
     RYLKTLKFLG YLDTDEHYFW LTHRVLRFSS SYLSSAHLPK VAQSFLNLLC AQTSLTFSIV
     VLDEHEVVPV ARSYLPQQDN LRVSPYGMHL GNRLPAHATS TGKVLLSVLD REVQIEWIEK
     YGLKRLTPYT ITDEHTFLET LDAVRQSDYC LSTEEHELGL IAIAVPVLNA QGLTIAALNC
     MSQTNRVQPQ YLIDQVLPLL RNTANELRNL V