TRMBR_THELN
ID TRMBR_THELN Reviewed; 338 AA.
AC Q7LYW4; H3ZP63;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=HTH-type sugar sensing transcriptional regulator TrmB;
DE AltName: Full=Transcriptional regulator of mal operon;
GN Name=trmB; ORFNames=OCC_03542;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
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 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [3]
RP FUNCTION, DNA-BINDING, 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] {ECO:0007744|PDB:2F5T}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 110-338 IN COMPLEX WITH MALTOSE,
RP SUBUNIT, AND DOMAIN.
RX PubMed=16473881; DOI=10.1074/jbc.m512809200;
RA Krug M., Lee S.J., Diederichs K., Boos W., Welte W.;
RT "Crystal structure of the sugar binding domain of the archaeal
RT transcriptional regulator TrmB.";
RL J. Biol. Chem. 281:10976-10982(2006).
CC -!- FUNCTION: Inhibits transcription of the trehalose/maltose transport
CC gene cluster (malE operon). Acts by binding to two different operator
CC sequences in the promoter, preventing polymerase recruitment and
CC transcription. {ECO:0000269|PubMed:12426307}.
CC -!- ACTIVITY REGULATION: Repressor activity is regulated by binding of
CC sugars to TrmB. Binding of maltose and trehalose results in
CC derepression of the malE operon. Maltose is much more effective (50-100
CC uM) than trehalose (2.5 mM). {ECO:0000269|PubMed:12426307}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16473881}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain and a C-terminal
CC sugar-binding domain. {ECO:0000269|PubMed:16473881}.
CC -!- SIMILARITY: Belongs to the transcriptional regulator TrmB family.
CC {ECO:0000305}.
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DR EMBL; AF307053; AAG45392.1; -; Genomic_DNA.
DR EMBL; CP006670; EHR78230.1; -; Genomic_DNA.
DR RefSeq; WP_004068718.1; NC_022084.1.
DR PDB; 2F5T; X-ray; 1.45 A; X=110-338.
DR PDBsum; 2F5T; -.
DR AlphaFoldDB; Q7LYW4; -.
DR SMR; Q7LYW4; -.
DR STRING; 523849.OCC_03542; -.
DR EnsemblBacteria; EHR78230; EHR78230; OCC_03542.
DR GeneID; 16548945; -.
DR KEGG; tlt:OCC_03542; -.
DR HOGENOM; CLU_062979_2_0_2; -.
DR OMA; VKREERC; -.
DR OrthoDB; 27311at2157; -.
DR EvolutionaryTrace; Q7LYW4; -.
DR Proteomes; UP000015502; 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; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..338
FT /note="HTH-type sugar sensing transcriptional regulator
FT TrmB"
FT /id="PRO_0000428842"
FT DNA_BIND 33..54
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="alpha-maltose"
FT /ligand_id="ChEBI:CHEBI:18167"
FT /evidence="ECO:0000269|PubMed:16473881,
FT ECO:0007744|PDB:2F5T"
FT BINDING 229
FT /ligand="alpha-maltose"
FT /ligand_id="ChEBI:CHEBI:18167"
FT /evidence="ECO:0000269|PubMed:16473881,
FT ECO:0007744|PDB:2F5T"
FT BINDING 305
FT /ligand="alpha-maltose"
FT /ligand_id="ChEBI:CHEBI:18167"
FT /evidence="ECO:0000269|PubMed:16473881,
FT ECO:0007744|PDB:2F5T"
FT BINDING 320..326
FT /ligand="alpha-maltose"
FT /ligand_id="ChEBI:CHEBI:18167"
FT /evidence="ECO:0000269|PubMed:16473881,
FT ECO:0007744|PDB:2F5T"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:2F5T"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:2F5T"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2F5T"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:2F5T"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:2F5T"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:2F5T"
FT TURN 204..208
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2F5T"
FT HELIX 221..236
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2F5T"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:2F5T"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2F5T"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 286..299
FT /evidence="ECO:0007829|PDB:2F5T"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:2F5T"
FT STRAND 325..337
FT /evidence="ECO:0007829|PDB:2F5T"
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
