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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)DescriptionActionsGraphical viewLength
Binding sitei205Maltose1 Publication1
Binding sitei229Maltose1 Publication1
Binding sitei305Maltose; via amide nitrogen and carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi33 – 54H-T-H motifSequence analysisAdd BLAST22

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004288421 – 338HTH-type sugar sensing transcriptional regulator TrmBAdd BLAST338

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi111 – 115Combined sources5
Helixi117 – 129Combined sources13
Beta strandi132 – 139Combined sources8
Helixi141 – 143Combined sources3
Helixi144 – 156Combined sources13
Beta strandi160 – 167Combined sources8
Helixi172 – 174Combined sources3
Beta strandi177 – 184Combined sources8
Beta strandi190 – 195Combined sources6
Turni196 – 198Combined sources3
Beta strandi199 – 203Combined sources5
Turni204 – 208Combined sources5
Beta strandi210 – 212Combined sources3
Beta strandi215 – 218Combined sources4
Helixi221 – 236Combined sources16
Beta strandi239 – 246Combined sources8
Beta strandi251 – 254Combined sources4
Helixi256 – 266Combined sources11
Turni267 – 269Combined sources3
Beta strandi272 – 280Combined sources9
Turni281 – 283Combined sources3
Beta strandi286 – 299Combined sources14
Turni300 – 303Combined sources4
Beta strandi304 – 311Combined sources8
Beta strandi314 – 319Combined sources6
Beta strandi325 – 337Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7LYW4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni189 – 190Maltose binding2
Regioni320 – 326Maltose binding7

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F5TX-ray1.45X110-338[»]
ProteinModelPortaliQ7LYW4.
SMRiQ7LYW4.
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...

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: November 2, 2016
This is version 54 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.