ID   TMBL1_PYRFU             Reviewed;         341 AA.
AC   Q8U4G4;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=HTH-type sugar sensing transcriptional regulator TrmBL1;
GN   Name=trmBL1; OrderedLocusNames=PF0124;
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).
RN   [2]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, SUBUNIT, INDUCTION, GENE NAME,
RP   AND MUTAGENESIS OF TYR-49 AND ASP-50.
RX   PubMed=17587231; DOI=10.1111/j.1365-2958.2007.05780.x;
RA   Lee S.J., Surma M., Seitz S., Hausner W., Thomm M., Boos W.;
RT   "Characterization of the TrmB-like protein, PF0124, a TGM-recognizing
RT   global transcriptional regulator of the hyperthermophilic archaeon
RT   Pyrococcus furiosus.";
RL   Mol. Microbiol. 65:305-318(2007).
CC   -!- FUNCTION: Global transcriptional repressor of the maltodextrin
CC       transport gene cluster (mdxE operon) and most likely of all genes
CC       encoding glycolytic enzymes. Acts by binding to the conserved TGM
CC       (Thermococcales-Glycolytic-Motif) sequences in their promoter region.
CC       Can also interact with non-TGM sequences.
CC       {ECO:0000269|PubMed:17587231}.
CC   -!- ACTIVITY REGULATION: Repressor activity is regulated by binding of
CC       different sugars to TrmBL1. Binding of maltose and maltotriose results
CC       in derepression of the target genes. However, high sugar concentration
CC       results in formation of octamers with high affinity for DNA, which may
CC       prevent transcription of target genes. {ECO:0000269|PubMed:17587231}.
CC   -!- SUBUNIT: Homotetramer. Forms homooctamers in the presence of
CC       maltotriose or maltose. {ECO:0000269|PubMed:17587231}.
CC   -!- INDUCTION: Autoregulated. {ECO:0000269|PubMed:17587231}.
CC   -!- DOMAIN: Contains an N-terminal DNA-binding domain and a C-terminal
CC       sugar-binding domain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transcriptional regulator TrmB family.
CC       {ECO:0000305}.
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DR   EMBL; AE009950; AAL80248.1; -; Genomic_DNA.
DR   RefSeq; WP_011011236.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U4G4; -.
DR   SMR; Q8U4G4; -.
DR   IntAct; Q8U4G4; 1.
DR   STRING; 186497.PF0124; -.
DR   PRIDE; Q8U4G4; -.
DR   EnsemblBacteria; AAL80248; AAL80248; PF0124.
DR   GeneID; 41711911; -.
DR   KEGG; pfu:PF0124; -.
DR   PATRIC; fig|186497.12.peg.129; -.
DR   eggNOG; arCOG02038; Archaea.
DR   HOGENOM; CLU_062979_2_0_2; -.
DR   OMA; GGAPWLM; -.
DR   OrthoDB; 65016at2157; -.
DR   PhylomeDB; Q8U4G4; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR021586; Tscrpt_reg_TrmB_C.
DR   InterPro; IPR002831; Tscrpt_reg_TrmB_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF11495; Regulator_TrmB; 1.
DR   Pfam; PF01978; TrmB; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..341
FT                   /note="HTH-type sugar sensing transcriptional regulator
FT                   TrmBL1"
FT                   /id="PRO_0000428840"
FT   DNA_BIND        32..53
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         49
FT                   /note="Y->N: Loss of DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:17587231"
FT   MUTAGEN         50
FT                   /note="D->N: Decreases DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:17587231"
SQ   SEQUENCE   341 AA;  39427 MW;  6D94DC1D059EBB26 CRC64;
     MLEEEILQKL QKFGLTKYES LAYLTLLKLG PSKATDVTKE SGIPHTRIYD VLSSLARKGF
     VDIVHGTPRL YAPVNPEIVL EKIREDLISD IERLKKAFQE LYREVHGEEL PEIWTVHGFE
     NTIDRAQHII RSAKHDILIN TPYEFLEYLR GVLEKRNDVL IIVISNFSEI PLWLRNKNNV
     ILARSGQAPW LLGTWVIGDI NYALFFGTLP EDKGKERFYS FWVKSTRLIQ NYVHWFYTMY
     FDNSEIVKPL NYERMEKPLT LSHIRTVITV LKQAGLPRNI EVIGRSLADK KQVTIKGKVI
     DYEYTPLTAN ITVKTDNKKI KVGGLGSYLE DIEGESFILL D