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Protein

PTS system trehalose-specific EIIBC component

Gene

treB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei29 – 291Phosphocysteine intermediate; for EIIB activityPROSITE-ProRule annotation

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 component
Alternative name(s):
EIIBC-Tre
Short name:
EII-Tre
Including the following 2 domains:
Trehalose-specific phosphotransferase enzyme IIB component (EC:2.7.1.201)
Alternative name(s):
PTS system trehalose-specific EIIB component
Trehalose permease IIC component
Alternative name(s):
PTS system trehalose-specific EIIC component
Gene namesi
Name:treB
Ordered Locus Names:b4240, JW4199
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12127. treB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 110110CytoplasmicSequence analysisAdd
BLAST
Transmembranei111 – 13121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini132 – 15827PeriplasmicSequence analysisAdd
BLAST
Transmembranei159 – 17921HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini180 – 1878CytoplasmicSequence analysis
Transmembranei188 – 20821HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini209 – 22517PeriplasmicSequence analysisAdd
BLAST
Transmembranei226 – 24621HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini247 – 25812CytoplasmicSequence analysisAdd
BLAST
Transmembranei259 – 27921HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini280 – 30021PeriplasmicSequence analysisAdd
BLAST
Transmembranei301 – 32121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini322 – 34019CytoplasmicSequence analysisAdd
BLAST
Transmembranei341 – 36121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini362 – 3709PeriplasmicSequence analysis
Transmembranei371 – 39121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini392 – 3987CytoplasmicSequence analysis
Transmembranei399 – 41921HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini420 – 44021PeriplasmicSequence analysisAdd
BLAST
Transmembranei441 – 46121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini462 – 47312CytoplasmicSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473PTS system trehalose-specific EIIBC componentPRO_0000186677Add
BLAST

Proteomic databases

PaxDbiP36672.
PRIDEiP36672.

Interactioni

Protein-protein interaction databases

BioGridi4262709. 7 interactions.
IntActiP36672. 1 interaction.
MINTiMINT-6478335.
STRINGi511145.b4240.

Structurei

3D structure databases

ProteinModelPortaliP36672.
SMRiP36672. Positions 11-92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8989PTS EIIB type-1PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 473365PTS EIIC type-1PROSITE-ProRule annotationAdd
BLAST

Domaini

The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

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.
OrthoDBiEOG6ND0GQ.
PhylomeDBiP36672.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1272GL → PF in AAC43381 (PubMed:7608078).Curated
Sequence conflicti184 – 19411GGTPILGIVLG → AQRRSLVSCLA in AAA97137 (PubMed:7610040).CuratedAdd
BLAST
Sequence conflicti187 – 1871Missing in AAC43381 (PubMed:7608078).Curated
Sequence conflicti307 – 3071A → Q in AAC43381 (PubMed:7608078).Curated
Sequence conflicti429 – 47345PGILS…TLDIV → RNSLDSTELLAGVCAGNGYR HHHPDCTHLVYLSAEIPPGH AGHCLIFFGAQLRSHSQE in AAC43381 (PubMed:7608078).CuratedAdd
BLAST

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. Positions 11-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262709. 7 interactions.
IntActiP36672. 1 interaction.
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.
OrthoDBiEOG6ND0GQ.
PhylomeDBiP36672.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP36672.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose."
    Klein W., Horlacher R., Boos W.
    J. Bacteriol. 177:4043-4052(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 184-194.
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.

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: July 6, 2016
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.