ID   NPHR_RHOSO              Reviewed;         335 AA.
AC   B1Q2A8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Transcriptional activator NphR;
GN   Name=nphR;
OS   Rhodococcus sp.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE DEGRADATION OF
RP   4-NITROPHENOL.
RC   STRAIN=PN1;
RX   PubMed=16233382; DOI=10.1263/jbb.95.139;
RA   Takeo M., Yasukawa T., Abe Y., Niihara S., Maeda Y., Negoro S.;
RT   "Cloning and characterization of a 4-nitrophenol hydroxylase gene cluster
RT   from Rhodococcus sp. PN1.";
RL   J. Biosci. Bioeng. 95:139-145(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR,
RP   AND INDUCTION.
RC   STRAIN=PN1;
RX   PubMed=18805976; DOI=10.1128/jb.00742-08;
RA   Takeo M., Murakami M., Niihara S., Yamamoto K., Nishimura M., Kato D.,
RA   Negoro S.;
RT   "Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. Strain PN1:
RT   characterization of the two-component 4-nitrophenol hydroxylase and
RT   regulation of its expression.";
RL   J. Bacteriol. 190:7367-7374(2008).
CC   -!- FUNCTION: Transcriptional activator of nphA1 and nphA2 involved in the
CC       degradation of 4-nitrophenol (4-NP). {ECO:0000269|PubMed:16233382,
CC       ECO:0000269|PubMed:18805976}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:18805976}.
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DR   EMBL; AB081773; BAG24015.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1Q2A8; -.
DR   SMR; B1Q2A8; -.
DR   PRIDE; B1Q2A8; -.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0046196; P:4-nitrophenol catabolic process; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   InterPro; IPR035418; AraC-bd_2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR   Pfam; PF14525; AraC_binding_2; 1.
DR   Pfam; PF12833; HTH_18; 1.
DR   PRINTS; PR00032; HTHARAC.
DR   SMART; SM00342; HTH_ARAC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..335
FT                   /note="Transcriptional activator NphR"
FT                   /id="PRO_0000418989"
FT   DOMAIN          231..329
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        249..270
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT   DNA_BIND        296..319
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
SQ   SEQUENCE   335 AA;  36441 MW;  F68E7CB70B2F8B1B CRC64;
     MAEREQSNDS ARTDVPAIVS LRTRELDTGE GRMQWASTLE RLYCETDVAW PEPRRHFDAE
     WGGRPFGDLH VSTIRADAHT VVRSPAMIQS DSGEGYLVCL VTDGSVEVRQ SGRATVVEPG
     SFALLDCAAP FVFHSPAPFR QVVVRSPREV LTSRLPGRIV EHGTARSIHG DTGAGGLVGR
     LFVDIADMDA PMSQGAAVSF ASSAVDMLAT ALTEGLLATS AADLHRTEDL TRVQRVIEQN
     LHDADITLSD IAAAAGMSLR TVHKLFNAEG TTTRAWLYQA RLEAARRYLL TTDLSVADVS
     ECAGFRDVSH FSRLFRSTFG SSPGLYRKEH ARIGS