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Protein

HTH-type sugar sensing transcriptional regulator TrmB

Gene

trmB

Organism
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits transcription of the trehalose/maltose transport gene cluster (malE operon). Acts by binding to two different operator sequences in the promoter, preventing polymerase recruitment and transcription.1 Publication

Enzyme regulationi

Repressor activity is regulated by binding of sugars to TrmB. Binding of maltose and trehalose results in derepression of the malE operon. Maltose is much more effective (50-100 µM) than trehalose (2.5 mM).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei205 – 2051Maltose1 Publication
Binding sitei229 – 2291Maltose1 Publication
Binding sitei305 – 3051Maltose; via amide nitrogen and carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi33 – 5422H-T-H motifSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type sugar sensing transcriptional regulator TrmB
Alternative name(s):
Transcriptional regulator of mal operon
Gene namesi
Name:trmB
ORF Names:OCC_03542
OrganismiThermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
Taxonomic identifieri523849 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
Proteomesi
  • UP000015502 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338HTH-type sugar sensing transcriptional regulator TrmBPRO_0000428842Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1155Combined sources
Helixi117 – 12913Combined sources
Beta strandi132 – 1398Combined sources
Helixi141 – 1433Combined sources
Helixi144 – 15613Combined sources
Beta strandi160 – 1678Combined sources
Helixi172 – 1743Combined sources
Beta strandi177 – 1848Combined sources
Beta strandi190 – 1956Combined sources
Turni196 – 1983Combined sources
Beta strandi199 – 2035Combined sources
Turni204 – 2085Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi215 – 2184Combined sources
Helixi221 – 23616Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi251 – 2544Combined sources
Helixi256 – 26611Combined sources
Turni267 – 2693Combined sources
Beta strandi272 – 2809Combined sources
Turni281 – 2833Combined sources
Beta strandi286 – 29914Combined sources
Turni300 – 3034Combined sources
Beta strandi304 – 3118Combined sources
Beta strandi314 – 3196Combined sources
Beta strandi325 – 33713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F5TX-ray1.45X110-338[»]
ProteinModelPortaliQ7LYW4.
SMRiQ7LYW4. Positions 110-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7LYW4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1902Maltose binding
Regioni320 – 3267Maltose binding

Domaini

Contains an N-terminal DNA-binding domain and a C-terminal sugar-binding domain.1 Publication

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR021586. Tscrpt_reg_TrmB_C.
IPR002831. Tscrpt_reg_TrmB_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF11495. Regulator_TrmB. 1 hit.
PF01978. TrmB. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7LYW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIPPEISHA LSEIGFTKYE ILTYWTLLVY GPSTAKEIST KSGIPYNRVY
60 70 80 90 100
DTISSLKLRG FVTEIEGTPK VYAAYSPRIA FFRFKKELED IMKKLEIELN
110 120 130 140 150
NVKKEEQRPA IWRSRSFDEA IEMFRESLYS AKNEVIVVTP SEFFETIRED
160 170 180 190 200
LIKTLERGVT VSLYIDKIPD LSEFKGKGNF FVRQFYKLNH LIGMTDGKEV
210 220 230 240 250
VTIQNATFDS IGPPSFKSTY PEIIFSQYSL IIEIFKESTL EKEIIGNPKD
260 270 280 290 300
IRFFAMFHAV DFVKNHLKNR NIYAEITGKN LESGRLETLT GRVVGYTLSL
310 320 330
REAVNNIHLE TENGVVKVGG MFAVIEDYES TEIKFIMG
Length:338
Mass (Da):38,839
Last modified:July 5, 2004 - v1
Checksum:iD7A7088C4528C715
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF307053 Genomic DNA. Translation: AAG45392.1.
CP006670 Genomic DNA. Translation: EHR78230.1.
RefSeqiWP_004068718.1. NC_022084.1.

Genome annotation databases

EnsemblBacteriaiEHR78230; EHR78230; OCC_03542.
GeneIDi16548945.
KEGGitlt:OCC_03542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF307053 Genomic DNA. Translation: AAG45392.1.
CP006670 Genomic DNA. Translation: EHR78230.1.
RefSeqiWP_004068718.1. NC_022084.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F5TX-ray1.45X110-338[»]
ProteinModelPortaliQ7LYW4.
SMRiQ7LYW4. Positions 110-338.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEHR78230; EHR78230; OCC_03542.
GeneIDi16548945.
KEGGitlt:OCC_03542.

Miscellaneous databases

EvolutionaryTraceiQ7LYW4.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR021586. Tscrpt_reg_TrmB_C.
IPR002831. Tscrpt_reg_TrmB_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF11495. Regulator_TrmB. 1 hit.
PF01978. TrmB. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  2. "Genome sequence of the model hyperthermophilic archaeon Thermococcus litoralis NS-C."
    Gardner A.F., Kumar S., Perler F.B.
    J. Bacteriol. 194:2375-2376(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51850 / DSM 5473 / JCM 8560 / NS-C.
  3. "TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis."
    Lee S.J., Engelmann A., Horlacher R., Qu Q., Vierke G., Hebbeln C., Thomm M., Boos W.
    J. Biol. Chem. 278:983-990(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, ENZYME REGULATION, GENE NAME.
  4. "Crystal structure of the sugar binding domain of the archaeal transcriptional regulator TrmB."
    Krug M., Lee S.J., Diederichs K., Boos W., Welte W.
    J. Biol. Chem. 281:10976-10982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 110-338 IN COMPLEX WITH MALTOSE, SUBUNIT, DOMAIN.

Entry informationi

Entry nameiTRMBR_THELN
AccessioniPrimary (citable) accession number: Q7LYW4
Secondary accession number(s): H3ZP63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.