ID   REG6_PYRFU              Reviewed;         151 AA.
AC   Q8U0P3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=HTH-type transcriptional regulator FL11 {ECO:0000250|UniProtKB:O59188};
DE   AltName: Full=Feast/famine regulatory protein FL11 {ECO:0000250|UniProtKB:O59188};
DE            Short=FFRP FL11 {ECO:0000250|UniProtKB:O59188};
GN   Name=fl11 {ECO:0000250|UniProtKB:O59188}; OrderedLocusNames=PF1543;
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 [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).
CC   -!- FUNCTION: DNA-binding protein involved in the repression of
CC       transcription of a large number of genes, thereby arresting growth, in
CC       response to environmental changes. {ECO:0000250|UniProtKB:O59188}.
CC   -!- ACTIVITY REGULATION: In the famine mode, FL11 forms dimers and acts as
CC       a repressor, leading to growth arrest. In the feast mode, in the
CC       presence of high concentrations of lysine or arginine, four dimers
CC       assemble into an octamer and cover the fl11 and lysine biosynthesis
CC       promoters. This leads to the inhibition of fl11 expression and lysine
CC       biosynthesis, decrease of the FL11 concentration in the cell,
CC       derepression of the target genes and activation of the metabolism.
CC       {ECO:0000250|UniProtKB:O59188}.
CC   -!- SUBUNIT: Homodimer. Binds DNA as a dimer and an octamer.
CC       {ECO:0000250|UniProtKB:O59188}.
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DR   EMBL; AE009950; AAL81667.1; -; Genomic_DNA.
DR   RefSeq; WP_011012690.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0P3; -.
DR   SMR; Q8U0P3; -.
DR   STRING; 186497.PF1543; -.
DR   PRIDE; Q8U0P3; -.
DR   EnsemblBacteria; AAL81667; AAL81667; PF1543.
DR   GeneID; 41713362; -.
DR   KEGG; pfu:PF1543; -.
DR   PATRIC; fig|186497.12.peg.1609; -.
DR   eggNOG; arCOG01580; Archaea.
DR   HOGENOM; CLU_091233_5_4_2; -.
DR   OMA; AGDENYI; -.
DR   OrthoDB; 97695at2157; -.
DR   PhylomeDB; Q8U0P3; -.
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; 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; PS50956; HTH_ASNC_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Reference proteome; Repressor; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..151
FT                   /note="HTH-type transcriptional regulator FL11"
FT                   /id="PRO_0000111768"
FT   DOMAIN          5..66
FT                   /note="HTH asnC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT   DNA_BIND        24..43
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT   BINDING         98..104
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:O59188"
FT   BINDING         118
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /evidence="ECO:0000250|UniProtKB:O59188"
FT   BINDING         122
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:O59188"
FT   BINDING         122
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /evidence="ECO:0000250|UniProtKB:O59188"
FT   BINDING         133..135
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:O59188"
FT   BINDING         133..135
FT                   /ligand="L-lysine"
FT                   /ligand_id="ChEBI:CHEBI:32551"
FT                   /evidence="ECO:0000250|UniProtKB:O59188"
SQ   SEQUENCE   151 AA;  17013 MW;  16853B7EF261AE8C CRC64;
     MRGILDDIDK KIIEILQKDG KVPLREISKI TGLAESTIHE RIKRLRESGV IKKFTAVVNP
     EALGYNILAF ILIKVKAGKY SEVASKLVKY PEIVEVYETT GDYDMVVKIR TKNSEELNNF
     LDMVGSIEGV EGTHTMIVLK VHKETTELPV K