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 27-MAR-2024, entry version 115.
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 PaxDb; 186497-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 OrthoDB; 6995at2157; -.
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; 3.30.70.920; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR30154; LEUCINE-RESPONSIVE REGULATORY PROTEIN; 1.
DR PANTHER; PTHR30154:SF34; TRANSCRIPTIONAL REGULATOR AZLB; 1.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR Pfam; PF13412; HTH_24; 1.
DR PRINTS; PR00033; HTHASNC.
DR SMART; SM00344; HTH_ASNC; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//
