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P31677

- OTSA_ECOLI

UniProt

P31677 - OTSA_ECOLI

Protein

Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

Gene

otsA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength.3 Publications

    Catalytic activityi

    UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

    Enzyme regulationi

    Activated by potassium and other monovalent cations at 0.25 M. Partially inhibited at greater concentrations.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Glucose-6-phosphate1 Publication
    Binding sitei77 – 771Glucose-6-phosphate1 Publication
    Sitei86 – 861Involved in alpha anomer selectivity
    Binding sitei131 – 1311Glucose-6-phosphate1 Publication
    Sitei156 – 1561Involved in alpha anomer selectivity
    Binding sitei263 – 2631UDP-glucose1 Publication
    Binding sitei268 – 2681UDP-glucose1 Publication
    Binding sitei301 – 3011Glucose-6-phosphate1 Publication
    Binding sitei340 – 3401UDP-glucose; via amide nitrogen and carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Source: EcoCyc

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: EcoliWiki
    2. response to osmotic stress Source: EcoCyc
    3. trehalose biosynthetic process Source: EcoCyc
    4. trehalose metabolism in response to cold stress Source: EcoCyc

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Potassium

    Enzyme and pathway databases

    BioCyciEcoCyc:TREHALOSE6PSYN-MONOMER.
    ECOL316407:JW5312-MONOMER.
    MetaCyc:TREHALOSE6PSYN-MONOMER.
    UniPathwayiUPA00299.

    Protein family/group databases

    CAZyiGT20. Glycosyltransferase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC:2.4.1.15)
    Alternative name(s):
    Osmoregulatory trehalose synthesis protein A
    Trehalose-6-phosphate synthase
    UDP-glucose-glucosephosphate glucosyltransferase
    Gene namesi
    Name:otsA
    Ordered Locus Names:b1896, JW5312
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11751. otsA.

    Pathology & Biotechi

    Disruption phenotypei

    Mutants are viable, but osmotically sensitive in minimal media and sensitive to cold shock.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 474473Alpha,alpha-trehalose-phosphate synthase [UDP-forming]PRO_0000122489Add
    BLAST

    Proteomic databases

    PaxDbiP31677.
    PRIDEiP31677.

    Expressioni

    Inductioni

    By cold-shock, osmotic-shock and during the transition to stationary phase. Expression is partially dependent on RpoS.4 Publications

    Gene expression databases

    GenevestigatoriP31677.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-10417N.
    STRINGi511145.b1896.

    Structurei

    Secondary structure

    1
    474
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Helixi16 – 183
    Helixi23 – 3513
    Beta strandi37 – 4711
    Beta strandi54 – 585
    Beta strandi61 – 688
    Helixi70 – 767
    Turni77 – 793
    Helixi80 – 834
    Helixi85 – 895
    Helixi93 – 953
    Helixi100 – 11718
    Helixi118 – 1203
    Beta strandi126 – 1316
    Helixi132 – 1343
    Helixi137 – 1437
    Beta strandi150 – 1534
    Helixi161 – 1644
    Helixi170 – 1778
    Beta strandi180 – 1878
    Helixi188 – 20114
    Beta strandi204 – 2074
    Turni208 – 2103
    Beta strandi211 – 2144
    Beta strandi217 – 2237
    Helixi230 – 2389
    Helixi243 – 2519
    Turni252 – 2543
    Beta strandi256 – 2616
    Helixi266 – 2683
    Helixi270 – 28314
    Helixi285 – 2873
    Turni288 – 2903
    Beta strandi291 – 2966
    Helixi305 – 32521
    Beta strandi332 – 3365
    Helixi342 – 35110
    Beta strandi353 – 3575
    Beta strandi360 – 3634
    Helixi366 – 3749
    Beta strandi382 – 3865
    Helixi390 – 3934
    Beta strandi398 – 4014
    Helixi406 – 41712
    Helixi421 – 43717
    Helixi440 – 45314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GZ5X-ray2.43A/B/C/D2-457[»]
    1UQTX-ray2.00A/B2-474[»]
    1UQUX-ray2.00A/B2-474[»]
    2WTXX-ray2.20A/B/C/D1-474[»]
    ProteinModelPortaliP31677.
    SMRiP31677. Positions 2-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31677.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 232UDP-glucose binding
    Regioni366 – 3705UDP-glucose binding

    Sequence similaritiesi

    Belongs to the glycosyltransferase 20 family.Curated

    Phylogenomic databases

    eggNOGiCOG0380.
    HOGENOMiHOG000191478.
    KOiK00697.
    OMAiWGESFVK.
    OrthoDBiEOG6CCH1M.
    PhylomeDBiP31677.

    Family and domain databases

    InterProiIPR001830. Glyco_trans_20.
    IPR012766. Trehalose_OtsA.
    [Graphical view]
    PfamiPF00982. Glyco_transf_20. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31677-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED    50
    QPLKKVKKGN ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR 100
    PAWDGYLRVN ALLADKLLPL LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI 150
    GFFLHIPFPT PEIFNALPTY DTLLEQLCDY DLLGFQTEND RLAFLDCLSN 200
    LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP LPPKLAQLKA 250
    ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS 300
    RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR 350
    YSDVGLVTPL RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI 400
    VNPYDRDEVA AALDRALTMS LAERISRHAE MLDVIVKNDI NHWQECFISD 450
    LKQIVPRSAE SQQRDKVATF PKLA 474
    Length:474
    Mass (Da):53,611
    Last modified:January 23, 2007 - v3
    Checksum:i63FFB6F938056F95
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69160 Genomic DNA. Translation: CAA48913.1.
    U00096 Genomic DNA. Translation: AAC74966.1.
    AP009048 Genomic DNA. Translation: BAA15717.2.
    U27211 Genomic DNA. Translation: AAA68604.1.
    PIRiI83402.
    RefSeqiNP_416410.1. NC_000913.3.
    YP_490157.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74966; AAC74966; b1896.
    BAA15717; BAA15717; BAA15717.
    GeneIDi12930479.
    946405.
    KEGGiecj:Y75_p1871.
    eco:b1896.
    PATRICi32119119. VBIEscCol129921_1977.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69160 Genomic DNA. Translation: CAA48913.1 .
    U00096 Genomic DNA. Translation: AAC74966.1 .
    AP009048 Genomic DNA. Translation: BAA15717.2 .
    U27211 Genomic DNA. Translation: AAA68604.1 .
    PIRi I83402.
    RefSeqi NP_416410.1. NC_000913.3.
    YP_490157.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GZ5 X-ray 2.43 A/B/C/D 2-457 [» ]
    1UQT X-ray 2.00 A/B 2-474 [» ]
    1UQU X-ray 2.00 A/B 2-474 [» ]
    2WTX X-ray 2.20 A/B/C/D 1-474 [» ]
    ProteinModelPortali P31677.
    SMRi P31677. Positions 2-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10417N.
    STRINGi 511145.b1896.

    Protein family/group databases

    CAZyi GT20. Glycosyltransferase Family 20.

    Proteomic databases

    PaxDbi P31677.
    PRIDEi P31677.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74966 ; AAC74966 ; b1896 .
    BAA15717 ; BAA15717 ; BAA15717 .
    GeneIDi 12930479.
    946405.
    KEGGi ecj:Y75_p1871.
    eco:b1896.
    PATRICi 32119119. VBIEscCol129921_1977.

    Organism-specific databases

    EchoBASEi EB1701.
    EcoGenei EG11751. otsA.

    Phylogenomic databases

    eggNOGi COG0380.
    HOGENOMi HOG000191478.
    KOi K00697.
    OMAi WGESFVK.
    OrthoDBi EOG6CCH1M.
    PhylomeDBi P31677.

    Enzyme and pathway databases

    UniPathwayi UPA00299 .
    BioCyci EcoCyc:TREHALOSE6PSYN-MONOMER.
    ECOL316407:JW5312-MONOMER.
    MetaCyc:TREHALOSE6PSYN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P31677.
    PROi P31677.

    Gene expression databases

    Genevestigatori P31677.

    Family and domain databases

    InterProi IPR001830. Glyco_trans_20.
    IPR012766. Trehalose_OtsA.
    [Graphical view ]
    Pfami PF00982. Glyco_transf_20. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02400. trehalose_OtsA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex."
      Kaasen I., McDougall J., Stroem A.R.
      Gene 145:9-15(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12 / CSH7.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      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. Estep P., O'Keeffe T., Robison K., Church G.M.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-474.
      Strain: K12 / EMG2.
    6. "Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: evidence that transcription is activated by katF (AppR)."
      Kaasen I., Falkenberg P., Styrvold O.B., Strom A.R.
      J. Bacteriol. 174:889-898(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, INDUCTION.
    7. "Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli."
      Giaever H.M., Styrvold O.B., Kaasen I., Stroem A.R.
      J. Bacteriol. 170:2841-2849(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, ENZYME REGULATION, DISRUPTION PHENOTYPE, INDUCTION, NOMENCLATURE.
    8. "Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli."
      Hengge-Aronis R., Klein W., Lange R., Rimmele M., Boos W.
      J. Bacteriol. 173:7918-7924(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures."
      Kandror O., DeLeon A., Goldberg A.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:9727-9732(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, INDUCTION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    10. "Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA."
      Gibson R.P., Turkenburg J.P., Charnock S.J., Lloyd R., Davies G.J.
      Chem. Biol. 9:1337-1346(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 1-457 IN COMPLEX WITH UDP AND GLUCOSE-6-PHOSPHATE, SUBUNIT.
    11. "The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution."
      Gibson R.P., Tarling C.A., Roberts S., Withers S.G., Davies G.J.
      J. Biol. Chem. 279:1950-1955(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH UDP-GLUCOSE AND SUBSTRATE ANALOG.

    Entry informationi

    Entry nameiOTSA_ECOLI
    AccessioniPrimary (citable) accession number: P31677
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3