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Protein

Trehalose operon transcriptional repressor

Gene

treR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Repressor for the trehalose operon (treP and treA). Binds trehalose-6-phosphate, which probably acts as an inducer.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi31 – 5020H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU07820-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Trehalose operon transcriptional repressor
Gene namesi
Name:treR
Synonyms:yfxA
Ordered Locus Names:BSU07820
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Trehalose operon transcriptional repressorPRO_0000050669Add
BLAST

Proteomic databases

PaxDbiP39796.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004353.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi97 – 1059Combined sources
Helixi109 – 1157Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi135 – 14511Combined sources
Turni146 – 1483Combined sources
Helixi154 – 1574Combined sources
Helixi161 – 1699Combined sources
Beta strandi172 – 18413Combined sources
Helixi187 – 1926Combined sources
Beta strandi200 – 21011Combined sources
Beta strandi215 – 22410Combined sources
Helixi225 – 2273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OGGX-ray2.50A90-238[»]
ProteinModelPortaliP39796.
SMRiP39796. Positions 2-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7171HTH gntR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH gntR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107414. Bacteria.
COG2188. LUCA.
HOGENOMiHOG000228718.
InParanoidiP39796.
KOiK03486.
OMAiNSIDNRQ.
OrthoDBiEOG689HVZ.
PhylomeDBiP39796.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.1410.10. 1 hit.
InterProiIPR028978. Chorismate_lyase_/UTRA_dom.
IPR012770. TreR.
IPR000524. Tscrpt_reg_HTH_GntR.
IPR011663. UTRA.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00392. GntR. 1 hit.
PF07702. UTRA. 1 hit.
[Graphical view]
PRINTSiPR00035. HTHGNTR.
SMARTiSM00345. HTH_GNTR. 1 hit.
SM00866. UTRA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF64288. SSF64288. 1 hit.
TIGRFAMsiTIGR02404. trehalos_R_Bsub. 1 hit.
PROSITEiPS50949. HTH_GNTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVNKFITIY KDIAQQIEGG RWKAEEILPS EHELTAQYGT SRETVRKALH
60 70 80 90 100
MLAQNGYIQK IRGKGSVVLN REKMQFPVSG LVSFKELAQT LGKETKTTVH
110 120 130 140 150
KFGLEPPSEL IQKQLRANLD DDIWEVIRSR KIDGEHVILD KDYFFRKHVP
160 170 180 190 200
HLTKEICENS IYEYIEGELG LSISYAQKEI VAEPCTDEDR ELLDLRGYDH
210 220 230
MVVVRNYVFL EDTSLFQYTE SRHRLDKFRF VDFARRGK
Length:238
Mass (Da):27,842
Last modified:October 1, 1996 - v2
Checksum:i41715DA057CEA600
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54245 Genomic DNA. Translation: CAA91016.1.
D83967 Genomic DNA. Translation: BAA23407.1.
AL009126 Genomic DNA. Translation: CAB12611.1.
X80203 Genomic DNA. Translation: CAA56496.1. Frameshift.
PIRiJC5038.
RefSeqiNP_388663.1. NC_000964.3.
WP_003233679.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12611; CAB12611; BSU07820.
GeneIDi936133.
KEGGibsu:BSU07820.
PATRICi18973212. VBIBacSub10457_0820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54245 Genomic DNA. Translation: CAA91016.1.
D83967 Genomic DNA. Translation: BAA23407.1.
AL009126 Genomic DNA. Translation: CAB12611.1.
X80203 Genomic DNA. Translation: CAA56496.1. Frameshift.
PIRiJC5038.
RefSeqiNP_388663.1. NC_000964.3.
WP_003233679.1. NZ_JNCM01000032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OGGX-ray2.50A90-238[»]
ProteinModelPortaliP39796.
SMRiP39796. Positions 2-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004353.

Proteomic databases

PaxDbiP39796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12611; CAB12611; BSU07820.
GeneIDi936133.
KEGGibsu:BSU07820.
PATRICi18973212. VBIBacSub10457_0820.

Phylogenomic databases

eggNOGiENOG4107414. Bacteria.
COG2188. LUCA.
HOGENOMiHOG000228718.
InParanoidiP39796.
KOiK03486.
OMAiNSIDNRQ.
OrthoDBiEOG689HVZ.
PhylomeDBiP39796.

Enzyme and pathway databases

BioCyciBSUB:BSU07820-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39796.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.1410.10. 1 hit.
InterProiIPR028978. Chorismate_lyase_/UTRA_dom.
IPR012770. TreR.
IPR000524. Tscrpt_reg_HTH_GntR.
IPR011663. UTRA.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00392. GntR. 1 hit.
PF07702. UTRA. 1 hit.
[Graphical view]
PRINTSiPR00035. HTHGNTR.
SMARTiSM00345. HTH_GNTR. 1 hit.
SM00866. UTRA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF64288. SSF64288. 1 hit.
TIGRFAMsiTIGR02404. trehalos_R_Bsub. 1 hit.
PROSITEiPS50949. HTH_GNTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of DNA flanking the treA gene of Bacillus subtilis reveals genes encoding a putative specific enzyme IITre and a potential regulator of the trehalose operon."
    Schoeck F., Dahl M.K.
    Gene 175:59-63(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  2. "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of the Bacillus subtilis chromosome containing genes for trehalose metabolism and acetoin utilization."
    Yamamoto H., Uchiyama S., Sekiguchi J.
    Microbiology 142:3057-3065(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / AC327.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a phospho-alpha-(1-1)-glucosidase encoded by the treA gene."
    Helfert C., Gotsche S., Dahl M.K.
    Mol. Microbiol. 16:111-120(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  5. "Expression of the tre operon of Bacillus subtilis 168 is regulated by the repressor TreR."
    Schoeck F., Dahl M.K.
    J. Bacteriol. 178:4576-4581(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiTRER_BACSU
AccessioniPrimary (citable) accession number: P39796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: February 17, 2016
This is version 119 of the entry and version 2 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.