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Protein

PTS system trehalose-specific EIIBC component

Gene

treB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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

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
  • trehalose transport Source: EcoCyc

Keywordsi

Molecular functionKinase, Transferase
Biological processPhosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:TREB-MONOMER
MetaCyc:TREB-MONOMER
SABIO-RKiP36672

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

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

PTM databases

iPTMnetiP36672

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, 12 interactors
IntActiP36672, 1 interactor
MINTiP36672
STRINGi316385.ECDH10B_4435

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C5Y Bacteria
COG1263 LUCA
COG1264 LUCA
HOGENOMiHOG000102022
InParanoidiP36672
KOiK02818
K02819
OMAiIGDIKMF
PhylomeDBiP36672

Family and domain databases

CDDicd00212 PTS_IIB_glc, 1 hit
Gene3Di3.30.1360.60, 1 hit
InterProiView protein in InterPro
IPR036878 Glu_permease_IIB
IPR018113 PTrfase_EIIB_Cys
IPR003352 PTS_EIIC
IPR013013 PTS_EIIC_1
IPR001996 PTS_IIB_1
IPR011296 PTS_IIBC_treh
IPR004719 PTS_maltose/Glc_sub_IIC
PfamiView protein in Pfam
PF00367 PTS_EIIB, 1 hit
PF02378 PTS_EIIC, 1 hit
SUPFAMiSSF55604 SSF55604, 1 hit
TIGRFAMsiTIGR00826 EIIB_glc, 1 hit
TIGR00852 pts-Glc, 1 hit
TIGR01992 PTS-IIBC-Tre, 1 hit
PROSITEiView protein in PROSITE
PS51098 PTS_EIIB_TYPE_1, 1 hit
PS01035 PTS_EIIB_TYPE_1_CYS, 1 hit
PS51103 PTS_EIIC_TYPE_1, 1 hit

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
WP_001407733.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77197; AAC77197; b4240
BAE78239; BAE78239; BAE78239
GeneIDi948761
KEGGiecj:JW4199
eco:b4240
PATRICifig|1411691.4.peg.2461

Similar proteinsi

Entry informationi

Entry nameiPTTBC_ECOLI
AccessioniPrimary (citable) accession number: P36672
Secondary accession number(s): Q2M667
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: March 28, 2018
This is version 155 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health