P62601 (TREF_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytoplasmic trehalase EC=3.2.1.28 Alternative name(s): Alpha,alpha-trehalase Alpha,alpha-trehalose glucohydrolase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 549 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. HAMAP-Rule MF_01059 |
| Catalytic activity | Alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose. HAMAP-Rule MF_01059 |
| Enzyme regulation | Activity decreases with increasing salt concentrations. HAMAP-Rule MF_01059 |
| Pathway | Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/1. HAMAP-Rule MF_01059 |
| Subunit structure | Monomer Probable. |
| Subcellular location | |
| Induction | Weakly induced by high osmolarity but not by trehalose. Expression is partially dependent on RpoS. HAMAP-Rule MF_01059 |
| Sequence similarities | Belongs to the glycosyl hydrolase 37 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 6.0. HAMAP-Rule MF_01059 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular hyperosmotic response Inferred from expression pattern PubMed 17015655. Source: EcoCyc trehalose catabolic processInferred from mutant phenotype Ref.4. Source: EcoCyc |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | alpha,alpha-trehalase activity Inferred from direct assay Ref.4. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 549 | 549 | Cytoplasmic trehalase HAMAP-Rule MF_01059 | PRO_0000173786 | |||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [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] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U00039 Genomic DNA. Translation: AAB18495.1. U00096 Genomic DNA. Translation: AAC76544.1. AP009048 Genomic DNA. Translation: BAE77775.1. |
| PIR | S47739. |
| RefSeq | NP_417976.1. NC_000913.2. YP_491916.1. NC_007779.1. |
3D structure databases | |
| ProteinModelPortal | P62601. |
| SMR | P62601. Positions 62-545. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P62601. 2 interactions. |
| STRING | 511145.b3519. |
Proteomic databases | |
| PRIDE | P62601. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC76544; AAC76544; b3519. BAE77775; BAE77775; BAE77775. |
| GeneID | 12931781. 948037. |
| KEGG | ecj:Y75_p3658. eco:b3519. |
| PATRIC | 32122500. VBIEscCol129921_3628. |
Organism-specific databases | |
| EchoBASE | EB2156. |
| EcoGene | EG12245. treF. |
Phylogenomic databases | |
| eggNOG | COG1626. |
| HOGENOM | HOG000215464. |
| KO | K01194. |
| OMA | FWMDGAD. |
| ProtClustDB | PRK13270. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:TREHALACYTO-MONOMER. ECOL316407:JW3487-MONOMER. MetaCyc:TREHALACYTO-MONOMER. |
| UniPathway | UPA00300; UER00535. |
Gene expression databases | |
| Genevestigator | P62601. |
Family and domain databases | |
| HAMAP | MF_01059. Cyt_trehalase. |
| InterPro | IPR008928. 6-hairpin_glycosidase-like. IPR023715. Cyt_trehalase. IPR001661. Glyco_hydro_37. IPR018232. Glyco_hydro_37_CS. [Graphical view] |
| PANTHER | PTHR23403. PTHR23403. 1 hit. |
| Pfam | PF01204. Trehalase. 1 hit. [Graphical view] |
| PRINTS | PR00744. GLHYDRLASE37. |
| SUPFAM | SSF48208. Glyco_trans_6hp. 1 hit. |
| PROSITE | PS00927. TREHALASE_1. 1 hit. PS00928. TREHALASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TREF_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P62601 Secondary accession number(s): P37196, Q2M7I1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
