ID   REG7_PYRHO              Reviewed;         141 AA.
AC   O59256;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=HTH-type transcriptional regulator LrpA;
GN   Name=lrpA; OrderedLocusNames=PH1592;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: DNA-binding protein that negatively regulates its own
CC       transcription. Interferes with RNA polymerase (RNAP) recruitment by
CC       inhibiting the association of RNAP with the TBP-TFB promoter complex.
CC       {ECO:0000250|UniProtKB:P42180}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC       {ECO:0000250|UniProtKB:P42180}.
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DR   EMBL; BA000001; BAA30704.1; -; Genomic_DNA.
DR   PIR; H71037; H71037.
DR   RefSeq; WP_010885666.1; NC_000961.1.
DR   AlphaFoldDB; O59256; -.
DR   SMR; O59256; -.
DR   STRING; 70601.3258021; -.
DR   EnsemblBacteria; BAA30704; BAA30704; BAA30704.
DR   GeneID; 1442445; -.
DR   KEGG; pho:PH1592; -.
DR   eggNOG; arCOG01580; Archaea.
DR   OMA; EDCWFIA; -.
DR   OrthoDB; 97695at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR000485; AsnC-type_HTH_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR   InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR   InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01037; AsnC_trans_reg; 1.
DR   PRINTS; PR00033; HTHASNC.
DR   SMART; SM00344; HTH_ASNC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS00519; HTH_ASNC_1; 1.
DR   PROSITE; PS50956; HTH_ASNC_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..141
FT                   /note="HTH-type transcriptional regulator LrpA"
FT                   /id="PRO_0000111772"
FT   DOMAIN          2..63
FT                   /note="HTH asnC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
SQ   SEQUENCE   141 AA;  15932 MW;  08B103E4B86078F9 CRC64;
     MIDERDKIIL EILSKDARTP FTEIAKKLGI SETAVRKRVK ALEEKGIIEG YTIRINPKKL
     GYSLVTITGV DTRPEKLFEV AEKLKEFEFV RELYLSSGDH MIMAVIWARD GEDLADIISN
     KIGKIDGVTK VCPAIILEKL K