REG6_PYRHO
ID REG6_PYRHO Reviewed; 151 AA.
AC O59188;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=HTH-type transcriptional regulator FL11 {ECO:0000305};
DE AltName: Full=Feast/famine regulatory protein FL11 {ECO:0000305};
DE Short=FFRP FL11 {ECO:0000305};
GN Name=fl11 {ECO:0000303|PubMed:14976242}; OrderedLocusNames=PH1519;
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).
RN [2] {ECO:0007744|PDB:1RI7}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, DNA-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=14976242; DOI=10.1073/pnas.0400109101;
RA Koike H., Ishijima S.A., Clowney L., Suzuki M.;
RT "The archaeal feast/famine regulatory protein: potential roles of its
RT assembly forms for regulating transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2840-2845(2004).
RN [3] {ECO:0007744|PDB:2CYY}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH L-GLUTAMINE.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RA Okazaki N., Nakano N., Shinkai A., Yokoyama S.;
RT "Crystal structure of PH1519 from Pyrococcus horikosii OT3.";
RL Submitted (JUL-2005) to the PDB data bank.
RN [4] {ECO:0007744|PDB:2E1C}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH DNA, FUNCTION,
RP ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=18073105; DOI=10.1016/j.str.2007.10.015;
RA Yokoyama K., Ishijima S.A., Koike H., Kurihara C., Shimowasa A.,
RA Kabasawa M., Kawashima T., Suzuki M.;
RT "Feast/famine regulation by transcription factor FL11 for the survival of
RT the hyperthermophilic archaeon Pyrococcus OT3.";
RL Structure 15:1542-1554(2007).
RN [5] {ECO:0007744|PDB:2ZNY, ECO:0007744|PDB:2ZNZ}
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF THE HOMOOCTAMER IN COMPLEXES WITH
RP L-ARGININE AND L-LYSINE, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=19004003; DOI=10.1002/prot.22269;
RA Yamada M., Ishijima S.A., Suzuki M.;
RT "Interactions between the archaeal transcription repressor FL11 and its
RT coregulators lysine and arginine.";
RL Proteins 74:520-525(2009).
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 (PubMed:14976242, PubMed:18073105).
CC Binding sites are identified in promoters of approximately 200
CC transcription units, including genes involved in ATP synthesis,
CC transmembrane transport, translation and DNA synthesis
CC (PubMed:18073105). {ECO:0000269|PubMed:14976242,
CC ECO:0000269|PubMed:18073105}.
CC -!- ACTIVITY REGULATION: In the famine mode, FL11 forms dimers and acts as
CC a repressor, leading to growth arrest (PubMed:18073105). In the feast
CC mode, in the presence of high concentrations of lysine or arginine,
CC four dimers assemble into an octamer and cover the fl11 and lysine
CC biosynthesis promoters (PubMed:18073105, PubMed:19004003). This leads
CC to the inhibition of fl11 expression and lysine biosynthesis, decrease
CC of the FL11 concentration in the cell, derepression of the target genes
CC and activation of the metabolism (PubMed:18073105).
CC {ECO:0000269|PubMed:18073105, ECO:0000269|PubMed:19004003}.
CC -!- SUBUNIT: Homodimer (PubMed:14976242, PubMed:18073105, PubMed:19004003).
CC Binds DNA as a dimer and an octamer (PubMed:18073105, PubMed:19004003).
CC The octamer formed with lysine is stable in solution, but the octamer
CC formed with arginine is unstable without DNA (PubMed:19004003). When
CC crystallized in the absence of DNA, dimers are assembled into helical
CC cylinders with six dimers per turn (PubMed:14976242). In solution,
CC predominantly behaves as a dimer (PubMed:14976242).
CC {ECO:0000269|PubMed:14976242, ECO:0000269|PubMed:18073105,
CC ECO:0000269|PubMed:19004003}.
CC -!- INTERACTION:
CC O59188; O59188: fl11; NbExp=5; IntAct=EBI-15665270, EBI-15665270;
CC O59188; O73983: PHS023; NbExp=2; IntAct=EBI-15665270, EBI-15665259;
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DR EMBL; BA000001; BAA30629.1; -; Genomic_DNA.
DR PIR; E71028; E71028.
DR RefSeq; WP_010885596.1; NC_000961.1.
DR PDB; 1RI7; X-ray; 2.70 A; A=1-151.
DR PDB; 2CYY; X-ray; 1.80 A; A=1-151.
DR PDB; 2E1C; X-ray; 2.10 A; A=1-151.
DR PDB; 2ZNY; X-ray; 2.59 A; A/B/C/D/E/F/G/H=1-151.
DR PDB; 2ZNZ; X-ray; 2.39 A; A/B/C/D/E/F/G/H=1-151.
DR PDBsum; 1RI7; -.
DR PDBsum; 2CYY; -.
DR PDBsum; 2E1C; -.
DR PDBsum; 2ZNY; -.
DR PDBsum; 2ZNZ; -.
DR AlphaFoldDB; O59188; -.
DR SMR; O59188; -.
DR IntAct; O59188; 1.
DR STRING; 70601.3257946; -.
DR EnsemblBacteria; BAA30629; BAA30629; BAA30629.
DR GeneID; 1443836; -.
DR KEGG; pho:PH1519; -.
DR eggNOG; arCOG01580; Archaea.
DR OMA; AGDENYI; -.
DR OrthoDB; 97695at2157; -.
DR EvolutionaryTrace; O59188; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 Pfam; PF13404; HTH_AsnC-type; 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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Repressor; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..151
FT /note="HTH-type transcriptional regulator FL11"
FT /id="PRO_0000111769"
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:0000269|PubMed:19004003,
FT ECO:0007744|PDB:2ZNY"
FT BINDING 118
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000269|PubMed:19004003,
FT ECO:0007744|PDB:2ZNZ"
FT BINDING 122
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:19004003,
FT ECO:0007744|PDB:2ZNY"
FT BINDING 122
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000269|PubMed:19004003,
FT ECO:0007744|PDB:2ZNZ"
FT BINDING 133..135
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:19004003,
FT ECO:0007744|PDB:2ZNY"
FT BINDING 133..135
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000269|PubMed:19004003,
FT ECO:0007744|PDB:2ZNZ"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:2CYY"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:2CYY"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:2CYY"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2CYY"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2ZNY"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2CYY"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:2CYY"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2CYY"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2CYY"
FT STRAND 100..113
FT /evidence="ECO:0007829|PDB:2CYY"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2CYY"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:2CYY"
SQ SEQUENCE 151 AA; 16954 MW; FD7BD105608588E6 CRC64;
MRVPLDEIDK KIIKILQNDG KAPLREISKI TGLAESTIHE RIRKLRESGV IKKFTAIIDP
EALGYSMLAF ILVKVKAGKY SEVASNLAKY PEIVEVYETT GDYDMVVKIR TKNSEELNNF
LDLIGSIPGV EGTHTMIVLK THKETTELPI K
