ID   REG7_PYRFU              Reviewed;         141 AA.
AC   P42180; Q9Y8K7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   25-MAY-2022, entry version 143.
DE   RecName: Full=HTH-type transcriptional regulator LrpA {ECO:0000305};
GN   Name=lrpA {ECO:0000303|PubMed:10973967}; OrderedLocusNames=PF1601;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=8406037; DOI=10.1016/0378-1119(93)90527-a;
RA   Eggen R.I.L., Geerling A.C.M., Waldkoetter K., Antranikian G., de Vos W.M.;
RT   "The glutamate dehydrogenase-encoding gene of the hyperthermophilic
RT   archaeon Pyrococcus furiosus: sequence, transcription and analysis of the
RT   deduced amino acid sequence.";
RL   Gene 132:143-148(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, FUNCTION,
RP   DNA-BINDING, AND SUBUNIT.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10973967; DOI=10.1074/jbc.m005916200;
RA   Brinkman A.B., Dahlke I., Tuininga J.E., Lammers T., Dumay V., de Heus E.,
RA   Lebbink J.H.G., Thomm M., de Vos W.M., van Der Oost J.;
RT   "An Lrp-like transcriptional regulator from the archaeon Pyrococcus
RT   furiosus is negatively autoregulated.";
RL   J. Biol. Chem. 275:38160-38169(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [4]
RP   IDENTIFICATION, AND SIMILARITY.
RX   PubMed=7770911; DOI=10.1016/s0968-0004(00)88988-4;
RA   Kyrpides N.C., Ouzounis C.A.;
RT   "The eubacterial transcriptional activator Lrp is present in the archaeon
RT   Pyrococcus furiosus.";
RL   Trends Biochem. Sci. 20:140-141(1995).
RN   [5]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=11809882; DOI=10.1093/nar/30.3.701;
RA   Dahlke I., Thomm M.;
RT   "A Pyrococcus homolog of the leucine-responsive regulatory protein, LrpA,
RT   inhibits transcription by abrogating RNA polymerase recruitment.";
RL   Nucleic Acids Res. 30:701-710(2002).
RN   [6]
RP   CRYSTALLIZATION, AND SUBUNIT.
RX   PubMed=11375518; DOI=10.1107/s0907444901005261;
RA   Sedelnikova S.E., Smits S.H., Leonard P.M., Brinkman A.B., van der Oost J.,
RA   Rafferty J.B., Rice D.W.;
RT   "Crystallization and quaternary structure analysis of an Lrp-like
RT   regulatory protein from the hyperthermophile Pyrococcus furiosus.";
RL   Acta Crystallogr. D 57:886-888(2001).
RN   [7] {ECO:0007744|PDB:1I1G}
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), SUBUNIT, AND DOMAIN.
RX   PubMed=11230123; DOI=10.1093/emboj/20.5.990;
RA   Leonard P.M., Smits S.H., Sedelnikova S.E., Brinkman A.B., de Vos W.M.,
RA   van der Oost J., Rice D.W., Rafferty J.B.;
RT   "Crystal structure of the Lrp-like transcriptional regulator from the
RT   archaeon Pyrococcus furiosus.";
RL   EMBO J. 20:990-997(2001).
CC   -!- FUNCTION: DNA-binding protein that negatively regulates its own
CC       transcription (PubMed:10973967, PubMed:11809882). Interferes with RNA
CC       polymerase (RNAP) recruitment by inhibiting the association of RNAP
CC       with the TBP-TFB promoter complex (PubMed:11809882). Binds to a 46-base
CC       pair sequence that overlaps the transcriptional start site of its own
CC       promoter (PubMed:10973967). {ECO:0000269|PubMed:10973967,
CC       ECO:0000269|PubMed:11809882}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers (PubMed:10973967,
CC       PubMed:11230123, PubMed:11375518). Forms a homodimer mainly through
CC       interactions between the antiparallel beta-sheets of the C-terminal
CC       domain, and further interactions lead to octamer formation
CC       (PubMed:11230123). {ECO:0000269|PubMed:11230123,
CC       ECO:0000305|PubMed:10973967, ECO:0000305|PubMed:11375518}.
CC   -!- DOMAIN: Consists of an N-terminal domain containing a helix-turn-helix
CC       (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta
CC       character reminiscent of a number of RNA- and DNA-binding domains.
CC       {ECO:0000269|PubMed:11230123}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M97860; AAD20389.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81725.1; -; Genomic_DNA.
DR   PIR; T46972; T46972.
DR   RefSeq; WP_011012747.1; NC_018092.1.
DR   PDB; 1I1G; X-ray; 2.90 A; A/B=1-141.
DR   PDBsum; 1I1G; -.
DR   AlphaFoldDB; P42180; -.
DR   SMR; P42180; -.
DR   STRING; 186497.PF1601; -.
DR   EnsemblBacteria; AAL81725; AAL81725; PF1601.
DR   GeneID; 41713425; -.
DR   KEGG; pfu:PF1601; -.
DR   PATRIC; fig|186497.12.peg.1667; -.
DR   eggNOG; arCOG01580; Archaea.
DR   HOGENOM; CLU_091233_5_4_2; -.
DR   OMA; EDCWFIA; -.
DR   OrthoDB; 97695at2157; -.
DR   PhylomeDB; P42180; -.
DR   EvolutionaryTrace; P42180; -.
DR   Proteomes; UP000001013; 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   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..141
FT                   /note="HTH-type transcriptional regulator LrpA"
FT                   /id="PRO_0000111771"
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"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   HELIX           21..28
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   HELIX           32..45
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   STRAND          64..72
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   STRAND          97..110
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   HELIX           111..120
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:1I1G"
FT   STRAND          128..135
FT                   /evidence="ECO:0007829|PDB:1I1G"
SQ   SEQUENCE   141 AA;  15892 MW;  41A74AD10119C925 CRC64;
     MIDERDKIIL EILEKDARTP FTEIAKKLGI SETAVRKRVK ALEEKGIIEG YTIKINPKKL
     GYSLVTITGV DTKPEKLFEV AEKLKEYDFV KELYLSSGDH MIMAVIWAKD GEDLAEIISN
     KIGKIEGVTK VCPAIILEKL K