Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytoplasmic trehalase

Gene

treF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity.

Catalytic activityi

Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose.UniRule annotation

Enzyme regulationi

Activity decreases with increasing salt concentrations.

pH dependencei

Optimum pH is 6.0.

Pathwayi: trehalose degradation

This protein is involved in step 1 of the subpathway that synthesizes D-glucose from alpha,alpha-trehalose.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Cytoplasmic trehalase (treF)
This subpathway is part of the pathway trehalose degradation, which is itself part of Glycan degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glucose from alpha,alpha-trehalose, the pathway trehalose degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681SubstrateUniRule annotation
Binding sitei212 – 2121SubstrateUniRule annotation
Binding sitei324 – 3241Substrate; via carbonyl oxygenUniRule annotation
Active sitei326 – 3261Proton donor/acceptorUniRule annotation
Active sitei509 – 5091Proton donor/acceptorUniRule annotation
Binding sitei525 – 5251SubstrateUniRule annotation

GO - Molecular functioni

  • alpha,alpha-trehalase activity Source: EcoCyc

GO - Biological processi

  • cellular hyperosmotic response Source: EcoCyc
  • trehalose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:TREHALACYTO-MONOMER.
ECOL316407:JW3487-MONOMER.
MetaCyc:TREHALACYTO-MONOMER.
UniPathwayiUPA00300; UER00535.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic trehalaseUniRule annotation (EC:3.2.1.28UniRule annotation)
Alternative name(s):
Alpha,alpha-trehalaseUniRule annotation
Alpha,alpha-trehalose glucohydrolaseUniRule annotation
Gene namesi
Name:treFUniRule annotation
Ordered Locus Names:b3519, JW3487
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12245. treF.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Cytoplasmic trehalasePRO_0000173786Add
BLAST

Proteomic databases

PaxDbiP62601.
PRIDEiP62601.

Expressioni

Inductioni

Weakly induced by high osmolarity but not by trehalose. Expression is partially dependent on RpoS.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

BioGridi4260775. 12 interactions.
IntActiP62601. 2 interactions.
STRINGi511145.b3519.

Structurei

3D structure databases

ProteinModelPortaliP62601.
SMRiP62601. Positions 62-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1762Substrate bindingUniRule annotation
Regioni221 – 2233Substrate bindingUniRule annotation
Regioni292 – 2943Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 37 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105E53. Bacteria.
COG1626. LUCA.
HOGENOMiHOG000215464.
InParanoidiP62601.
KOiK01194.
OMAiFWMDGAD.
OrthoDBiEOG6CCH1S.
PhylomeDBiP62601.

Family and domain databases

HAMAPiMF_01059. Cyt_trehalase.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR023715. Cyt_trehalase.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62601-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNQKIQNPN PDELMIEVDL CYELDPYELK LDEMIEAEPE PEMIEGLPAS
60 70 80 90 100
DALTPADRYL ELFEHVQSAK IFPDSKTFPD CAPKMDPLDI LIRYRKVRRH
110 120 130 140 150
RDFDLRKFVE NHFWLPEVYS SEYVSDPQNS LKEHIDQLWP VLTREPQDHI
160 170 180 190 200
PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT MLGLAESGRE DLLKCMADNF
210 220 230 240 250
AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR GARRYLDHLK
260 270 280 290 300
MEYAFWMDGA ESLIPNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV
310 320 330 340 350
ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDTGRLAS IRTTQFIPID
360 370 380 390 400
LNAFLFKLES AIANISALKG EKETEALFRQ KASARRDAVN RYLWDDENGI
410 420 430 440 450
YRDYDWRREQ LALFSAAAIV PLYVGMANHE QADRLANAVR SRLLTPGGIL
460 470 480 490 500
ASEYETGEQW DKPNGWAPLQ WMAIQGFKMY GDDLLGDEIA RSWLKTVNQF
510 520 530 540
YLEQHKLIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR RLIGLYGEP
Length:549
Mass (Da):63,697
Last modified:July 19, 2004 - v1
Checksum:i543B82A7FAD4CB9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18495.1.
U00096 Genomic DNA. Translation: AAC76544.1.
AP009048 Genomic DNA. Translation: BAE77775.1.
PIRiS47739.
RefSeqiNP_417976.1. NC_000913.3.
WP_000934216.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76544; AAC76544; b3519.
BAE77775; BAE77775; BAE77775.
GeneIDi948037.
KEGGiecj:JW3487.
eco:b3519.
PATRICi32122500. VBIEscCol129921_3628.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18495.1.
U00096 Genomic DNA. Translation: AAC76544.1.
AP009048 Genomic DNA. Translation: BAE77775.1.
PIRiS47739.
RefSeqiNP_417976.1. NC_000913.3.
WP_000934216.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP62601.
SMRiP62601. Positions 62-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260775. 12 interactions.
IntActiP62601. 2 interactions.
STRINGi511145.b3519.

Proteomic databases

PaxDbiP62601.
PRIDEiP62601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76544; AAC76544; b3519.
BAE77775; BAE77775; BAE77775.
GeneIDi948037.
KEGGiecj:JW3487.
eco:b3519.
PATRICi32122500. VBIEscCol129921_3628.

Organism-specific databases

EchoBASEiEB2156.
EcoGeneiEG12245. treF.

Phylogenomic databases

eggNOGiENOG4105E53. Bacteria.
COG1626. LUCA.
HOGENOMiHOG000215464.
InParanoidiP62601.
KOiK01194.
OMAiFWMDGAD.
OrthoDBiEOG6CCH1S.
PhylomeDBiP62601.

Enzyme and pathway databases

UniPathwayiUPA00300; UER00535.
BioCyciEcoCyc:TREHALACYTO-MONOMER.
ECOL316407:JW3487-MONOMER.
MetaCyc:TREHALACYTO-MONOMER.

Miscellaneous databases

PROiP62601.

Family and domain databases

HAMAPiMF_01059. Cyt_trehalase.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR023715. Cyt_trehalase.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
PANTHERiPTHR23403. PTHR23403. 1 hit.
PfamiPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSiPR00744. GLHYDRLASE37.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Characterization of a cytoplasmic trehalase of Escherichia coli."
    Horlacher R., Uhland K., Klein W., Ehrmann M., Boos W.
    J. Bacteriol. 178:6250-6257(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF N-TERMINUS.
    Strain: DHB4 and K12 / MC4100 / ATCC 35695 / DSM 6574.
  5. "Determinants of translocation and folding of TreF, a trehalase of Escherichia coli."
    Uhland K., Mondigler M., Spiess C., Prinz W., Ehrmann M.
    J. Biol. Chem. 275:23439-23445(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: DHB3 and K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiTREF_ECOLI
AccessioniPrimary (citable) accession number: P62601
Secondary accession number(s): P37196, Q2M7I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: January 20, 2016
This is version 85 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.