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Protein

PTS system trehalose-specific EIIBC component

Gene

treB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport at low osmolarity.1 Publication1 Publication

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + alpha,alpha-trehalose(Side 1) = [protein]-L-histidine + alpha,alpha-trehalose 6-phosphate(Side 2).1 Publication

Kineticsi

  1. KM=16 µM for trehalose1 Publication
  1. Vmax=9 nmol/min/mg enzyme toward trehalose1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei29Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
  • regulation of carbohydrate utilization Source: GO_Central
  • trehalose transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:TREB-MONOMER.
ECOL316407:JW4199-MONOMER.
MetaCyc:TREB-MONOMER.

Protein family/group databases

TCDBi4.A.1.2.4. the pts glucose-glucoside (glc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
PTS system trehalose-specific EIIBC component1 Publication
Alternative name(s):
EIIBC-Tre1 Publication
Short name:
EII-Tre1 Publication
Including the following 2 domains:
Trehalose-specific phosphotransferase enzyme IIB component1 Publication (EC:2.7.1.2011 Publication)
Alternative name(s):
PTS system trehalose-specific EIIB component1 Publication
Trehalose permease IIC component1 Publication
Alternative name(s):
PTS system trehalose-specific EIIC component1 Publication
Gene namesi
Name:treB
Ordered Locus Names:b4240, JW4199
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12127. treB.

Subcellular locationi

  • Cell inner membrane PROSITE-ProRule annotation1 Publication; Multi-pass membrane protein PROSITE-ProRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 110CytoplasmicSequence analysisAdd BLAST110
Transmembranei111 – 131HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini132 – 158PeriplasmicSequence analysisAdd BLAST27
Transmembranei159 – 179HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini180 – 187CytoplasmicSequence analysis8
Transmembranei188 – 208HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini209 – 225PeriplasmicSequence analysisAdd BLAST17
Transmembranei226 – 246HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini247 – 258CytoplasmicSequence analysisAdd BLAST12
Transmembranei259 – 279HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini280 – 300PeriplasmicSequence analysisAdd BLAST21
Transmembranei301 – 321HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini322 – 340CytoplasmicSequence analysisAdd BLAST19
Transmembranei341 – 361HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini362 – 370PeriplasmicSequence analysis9
Transmembranei371 – 391HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini392 – 398CytoplasmicSequence analysis7
Transmembranei399 – 419HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini420 – 440PeriplasmicSequence analysisAdd BLAST21
Transmembranei441 – 461HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini462 – 473CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001866771 – 473PTS system trehalose-specific EIIBC componentAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29Phosphocysteine; by EIIA1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP36672.
PRIDEiP36672.

Expressioni

Inductioni

At low osmolarity, treB is induced by trehalose-6-phosphate, but it becomes uninducible at high osmolarity due to induction of trehalose-6-phosphate phosphatase OstB which is part of the biosynthetic pathway of trehalose synthesis at high osmolarity. Repressed by TreR.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4262709. 7 interactors.
IntActiP36672. 1 interactor.
MINTiMINT-6478335.
STRINGi511145.b4240.

Structurei

3D structure databases

ProteinModelPortaliP36672.
SMRiP36672.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 89PTS EIIB type-1PROSITE-ProRule annotationAdd BLAST89
Domaini109 – 473PTS EIIC type-1PROSITE-ProRule annotationAdd BLAST365

Domaini

The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA-Glc (EIII-Glc) on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain.PROSITE-ProRule annotation1 Publication
The EIIC domain type-1 forms the PTS system translocation channel and contains the specific substrate-binding site.PROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 PTS EIIB type-1 domain.PROSITE-ProRule annotation
Contains 1 PTS EIIC type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG1263. LUCA.
COG1264. LUCA.
HOGENOMiHOG000102022.
InParanoidiP36672.
KOiK02818.
K02819.
OMAiVIGDIKM.
PhylomeDBiP36672.

Family and domain databases

CDDicd00212. PTS_IIB_glc. 1 hit.
Gene3Di3.30.1360.60. 1 hit.
InterProiIPR018113. PTrfase_EIIB_Cys.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR011296. PTS_IIBC_treh.
IPR004719. PTS_maltose/Glc_sub_IIC.
[Graphical view]
PfamiPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR01992. PTS-IIBC-Tre. 1 hit.
PROSITEiPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSKINQTDI DRLIELVGGR GNIATVSHCI TRLRFVLNQP ANARPKEIEQ
60 70 80 90 100
LPMVKGCFTN AGQFQVVIGT NVGDYYQALI ASTGQAQVDK EQVKKAARHN
110 120 130 140 150
MKWHEQLISH FAVIFFPLLP ALISGGLILG FRNVIGDLPM SNGQTLAQMY
160 170 180 190 200
PSLQTIYDFL WLIGEAIFFY LPVGICWSAV KKMGGTPILG IVLGVTLVSP
210 220 230 240 250
QLMNAYLLGQ QLPEVWDFGM FSIAKVGYQA QVIPALLAGL ALGVIETRLK
260 270 280 290 300
RIVPDYLYLV VVPVCSLILA VFLAHALIGP FGRMIGDGVA FAVRHLMTGS
310 320 330 340 350
FAPIGAALFG FLYAPLVITG VHQTTLAIDL QMIQSMGGTP VWPLIALSNI
360 370 380 390 400
AQGSAVIGII ISSRKHNERE ISVPAAISAW LGVTEPAMYG INLKYRFPML
410 420 430 440 450
CAMIGSGLAG LLCGLNGVMA NGIGVGGLPG ILSIQPSYWQ VFALAMAIAI
460 470
IIPIVLTSFI YQRKYRLGTL DIV
Length:473
Mass (Da):51,081
Last modified:July 15, 1998 - v4
Checksum:i7437F8822B624944
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti126 – 127GL → PF in AAC43381 (PubMed:7608078).Curated2
Sequence conflicti184 – 194GGTPILGIVLG → AQRRSLVSCLA in AAA97137 (PubMed:7610040).CuratedAdd BLAST11
Sequence conflicti187Missing in AAC43381 (PubMed:7608078).Curated1
Sequence conflicti307A → Q in AAC43381 (PubMed:7608078).Curated1
Sequence conflicti429 – 473PGILS…TLDIV → RNSLDSTELLAGVCAGNGYR HHHPDCTHLVYLSAEIPPGH AGHCLIFFGAQLRSHSQE in AAC43381 (PubMed:7608078).CuratedAdd BLAST45

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06195 Genomic DNA. Translation: AAC43381.1.
U14003 Genomic DNA. Translation: AAA97137.1.
U00096 Genomic DNA. Translation: AAC77197.1.
AP009048 Genomic DNA. Translation: BAE78239.1.
PIRiC65236.
RefSeqiNP_418661.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC77197; AAC77197; b4240.
BAE78239; BAE78239; BAE78239.
GeneIDi948761.
KEGGiecj:JW4199.
eco:b4240.
PATRICi32124055. VBIEscCol129921_4372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06195 Genomic DNA. Translation: AAC43381.1.
U14003 Genomic DNA. Translation: AAA97137.1.
U00096 Genomic DNA. Translation: AAC77197.1.
AP009048 Genomic DNA. Translation: BAE78239.1.
PIRiC65236.
RefSeqiNP_418661.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP36672.
SMRiP36672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262709. 7 interactors.
IntActiP36672. 1 interactor.
MINTiMINT-6478335.
STRINGi511145.b4240.

Protein family/group databases

TCDBi4.A.1.2.4. the pts glucose-glucoside (glc) family.

Proteomic databases

PaxDbiP36672.
PRIDEiP36672.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77197; AAC77197; b4240.
BAE78239; BAE78239; BAE78239.
GeneIDi948761.
KEGGiecj:JW4199.
eco:b4240.
PATRICi32124055. VBIEscCol129921_4372.

Organism-specific databases

EchoBASEiEB2048.
EcoGeneiEG12127. treB.

Phylogenomic databases

eggNOGiENOG4105C5Y. Bacteria.
COG1263. LUCA.
COG1264. LUCA.
HOGENOMiHOG000102022.
InParanoidiP36672.
KOiK02818.
K02819.
OMAiVIGDIKM.
PhylomeDBiP36672.

Enzyme and pathway databases

BioCyciEcoCyc:TREB-MONOMER.
ECOL316407:JW4199-MONOMER.
MetaCyc:TREB-MONOMER.

Miscellaneous databases

PROiP36672.

Family and domain databases

CDDicd00212. PTS_IIB_glc. 1 hit.
Gene3Di3.30.1360.60. 1 hit.
InterProiIPR018113. PTrfase_EIIB_Cys.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
IPR001996. PTS_IIB_1.
IPR011296. PTS_IIBC_treh.
IPR004719. PTS_maltose/Glc_sub_IIC.
[Graphical view]
PfamiPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMiSSF55604. SSF55604. 1 hit.
TIGRFAMsiTIGR00826. EIIB_glc. 1 hit.
TIGR00852. pts-Glc. 1 hit.
TIGR01992. PTS-IIBC-Tre. 1 hit.
PROSITEiPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTTBC_ECOLI
AccessioniPrimary (citable) accession number: P36672
Secondary accession number(s): Q2M667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

E.coli does not possess a trehalose-specific phosphotransferase enzyme IIA component, however it seems that it use the glucose-specific phosphotransferase enzyme IIA component to delivers trehalose-6-phosphate into the cell.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.