TRMBR_PYRFU
ID TRMBR_PYRFU Reviewed; 338 AA.
AC Q9HGZ9; E7FHI4; Q7LYC7;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=HTH-type sugar sensing transcriptional regulator TrmB;
GN Name=trmB; OrderedLocusNames=PF1743;
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=11115105; DOI=10.1046/j.1365-2958.2000.02161.x;
RA Diruggiero J., Dunn D., Maeder D.L., Holley-Shanks R., Chatard J.,
RA Horlacher R., Robb F.T., Boos W., Weiss R.B.;
RT "Evidence of recent lateral gene transfer among hyperthermophilic
RT archaea.";
RL Mol. Microbiol. 38:684-693(2000).
RN [2]
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 [3]
RP FUNCTION, ACTIVITY REGULATION, AND GENE NAME.
RX PubMed=12426307; DOI=10.1074/jbc.m210236200;
RA Lee S.J., Engelmann A., Horlacher R., Qu Q., Vierke G., Hebbeln C.,
RA Thomm M., Boos W.;
RT "TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose
RT ABC transporter from the hyperthermophilic archaeon Thermococcus
RT litoralis.";
RL J. Biol. Chem. 278:983-990(2003).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=16135241; DOI=10.1111/j.1365-2958.2005.04804.x;
RA Lee S.J., Moulakakis C., Koning S.M., Hausner W., Thomm M., Boos W.;
RT "TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus
RT furiosus exhibits dual promoter specificity and is controlled by different
RT inducers.";
RL Mol. Microbiol. 57:1797-1807(2005).
RN [5]
RP ACTIVITY REGULATION, DNA-BINDING, AND MUTAGENESIS OF TYR-50 AND THR-52.
RX PubMed=17504272; DOI=10.1111/j.1365-2958.2007.05737.x;
RA Lee S.J., Surma M., Seitz S., Hausner W., Thomm M., Boos W.;
RT "Differential signal transduction via TrmB, a sugar sensing transcriptional
RT repressor of Pyrococcus furiosus.";
RL Mol. Microbiol. 64:1499-1505(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) IN COMPLEX WITH SUCROSE, SUBUNIT,
RP AND DOMAIN.
RX PubMed=23576322; DOI=10.1002/pro.2263;
RA Krug M., Lee S.J., Boos W., Diederichs K., Welte W.;
RT "The three-dimensional structure of TrmB, a transcriptional regulator of
RT dual function in the hyperthermophilic archaeon Pyrococcus furiosus in
RT complex with sucrose.";
RL Protein Sci. 22:800-808(2013).
CC -!- FUNCTION: Inhibits transcription of the trehalose/maltose transport
CC gene cluster (malE operon) and of the maltodextrin transport gene
CC cluster (mdxE operon). Acts by binding to two different operator
CC sequences in both promoters, preventing polymerase recruitment and
CC transcription. {ECO:0000269|PubMed:12426307,
CC ECO:0000269|PubMed:16135241}.
CC -!- ACTIVITY REGULATION: Repressor activity is regulated by binding of
CC different sugars to TrmB. These sugars can act as inducers or
CC corepressors. Binding of maltose and trehalose results in derepression
CC of the malE operon, and binding of maltotriose, larger maltodextrins
CC and, to a minor extent, sucrose results in derepression of the mdxE
CC operon. In contrast, binding of glucose causes stronger repression of
CC the malE and mdxE operons. Maltose may also act as a corepressor of the
CC mdxE operon. {ECO:0000269|PubMed:12426307, ECO:0000269|PubMed:16135241,
CC ECO:0000269|PubMed:17504272}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16135241,
CC ECO:0000269|PubMed:23576322}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain and a C-terminal
CC sugar-binding domain. {ECO:0000269|PubMed:23576322}.
CC -!- SIMILARITY: Belongs to the transcriptional regulator TrmB family.
CC {ECO:0000305}.
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DR EMBL; AF307052; AAG45376.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81867.1; -; Genomic_DNA.
DR RefSeq; WP_004068718.1; NC_003413.1.
DR PDB; 3QPH; X-ray; 2.99 A; A=1-338.
DR PDBsum; 3QPH; -.
DR AlphaFoldDB; Q9HGZ9; -.
DR SMR; Q9HGZ9; -.
DR STRING; 186497.PF1743; -.
DR EnsemblBacteria; AAL81867; AAL81867; PF1743.
DR GeneID; 16548945; -.
DR KEGG; pfu:PF1743; -.
DR PATRIC; fig|186497.12.peg.1812; -.
DR eggNOG; arCOG02038; Archaea.
DR HOGENOM; CLU_062979_2_0_2; -.
DR OMA; VKREERC; -.
DR OrthoDB; 27311at2157; -.
DR PhylomeDB; Q9HGZ9; -.
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 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..338
FT /note="HTH-type sugar sensing transcriptional regulator
FT TrmB"
FT /id="PRO_0000428839"
FT DNA_BIND 33..54
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 303..305
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT BINDING 321..326
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT MUTAGEN 50
FT /note="Y->N: Loss of DNA-binding."
FT /evidence="ECO:0000269|PubMed:17504272"
FT MUTAGEN 52
FT /note="T->K: Decreases DNA-binding."
FT /evidence="ECO:0000269|PubMed:17504272"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 77..100
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3QPH"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 221..237
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3QPH"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:3QPH"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:3QPH"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 286..299
FT /evidence="ECO:0007829|PDB:3QPH"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:3QPH"
FT STRAND 325..337
FT /evidence="ECO:0007829|PDB:3QPH"
SQ SEQUENCE 338 AA; 38839 MW; D7A7088C4528C715 CRC64;
MEIPPEISHA LSEIGFTKYE ILTYWTLLVY GPSTAKEIST KSGIPYNRVY DTISSLKLRG
FVTEIEGTPK VYAAYSPRIA FFRFKKELED IMKKLEIELN NVKKEEQRPA IWRSRSFDEA
IEMFRESLYS AKNEVIVVTP SEFFETIRED LIKTLERGVT VSLYIDKIPD LSEFKGKGNF
FVRQFYKLNH LIGMTDGKEV VTIQNATFDS IGPPSFKSTY PEIIFSQYSL IIEIFKESTL
EKEIIGNPKD IRFFAMFHAV DFVKNHLKNR NIYAEITGKN LESGRLETLT GRVVGYTLSL
REAVNNIHLE TENGVVKVGG MFAVIEDYES TEIKFIMG
