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Protein

Trehalose-6-phosphate phosphatase

Gene

otsB

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

Functioni

Removes the phosphate from trehalose 6-phosphate (Tre6P) to produce free trehalose. Also catalyzes the dephosphorylation of glucose-6-phosphate (Glu6P) and 2-deoxyglucose-6-phosphate (2dGlu6P).2 Publications

Catalytic activityi

Trehalose 6-phosphate + H2O = trehalose + phosphate.

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication, Zn2+1 PublicationNote: Magnesium. Can also use other divalent metal cations as manganese, cobalt or zinc.1 Publication

Kineticsi

  1. KM=0.61 mM for Tre6P (with magnesium ions as cofactor and at pH 9)1 Publication

    pH dependencei

    Optimum pH is between 6 and 7.5.1 Publication

    Pathwayi: trehalose biosynthesis

    This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei20 – 201NucleophileBy similarity
    Metal bindingi20 – 201MagnesiumBy similarity
    Metal bindingi22 – 221Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi198 – 1981MagnesiumBy similarity

    GO - Molecular functioni

    • magnesium ion binding Source: UniProtKB
    • trehalose-phosphatase activity Source: EcoCyc

    GO - Biological processi

    • dephosphorylation Source: GOC
    • response to osmotic stress Source: EcoCyc
    • trehalose biosynthetic process Source: EcoCyc
    • trehalose metabolism in response to cold stress Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:TREHALOSEPHOSPHASYN-MONOMER.
    ECOL316407:JW1886-MONOMER.
    MetaCyc:TREHALOSEPHOSPHASYN-MONOMER.
    UniPathwayiUPA00299.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trehalose-6-phosphate phosphatase (EC:3.1.3.12)
    Short name:
    TPP
    Alternative name(s):
    Osmoregulatory trehalose synthesis protein B
    Trehalose 6-phosphate phosphatase
    Trehalose-phosphatase
    Gene namesi
    Name:otsB
    Ordered Locus Names:b1897, JW1886
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11752. otsB.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 266266Trehalose-6-phosphate phosphatasePRO_0000058100Add
    BLAST

    Proteomic databases

    PaxDbiP31678.

    2D gel databases

    SWISS-2DPAGEP31678.

    Expressioni

    Inductioni

    By cold-shock, osmotic-shock and during the transition to stationary phase. Expression is partially dependent on RpoS.5 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi4262243. 10 interactions.
    IntActiP31678. 15 interactions.
    STRINGi511145.b1897.

    Structurei

    3D structure databases

    ProteinModelPortaliP31678.
    SMRiP31678. Positions 18-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 223Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the trehalose phosphatase family.Curated

    Phylogenomic databases

    eggNOGiENOG4108K4C. Bacteria.
    COG1877. LUCA.
    HOGENOMiHOG000239290.
    InParanoidiP31678.
    KOiK01087.
    OMAiWAMFLDI.
    OrthoDBiEOG6T7NBK.
    PhylomeDBiP31678.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR003337. Trehalose_PPase.
    [Graphical view]
    PfamiPF02358. Trehalose_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    TIGR00685. T6PP. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P31678-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTEPLTETPE LSAKYAWFFD LDGTLAEIKP HPDQVVVPDN ILQGLQLLAT
    60 70 80 90 100
    ASDGALALIS GRSMVELDAL AKPYRFPLAG VHGAERRDIN GKTHIVHLPD
    110 120 130 140 150
    AIARDISVQL HTVIAQYPGA ELEAKGMAFA LHYRQAPQHE DALMTLAQRI
    160 170 180 190 200
    TQIWPQMALQ QGKCVVEIKP RGTSKGEAIA AFMQEAPFIG RTPVFLGDDL
    210 220 230 240 250
    TDESGFAVVN RLGGMSVKIG TGATQASWRL AGVPDVWSWL EMITTALQQK
    260
    RENNRSDDYE SFSRSI
    Length:266
    Mass (Da):29,175
    Last modified:February 1, 1995 - v2
    Checksum:i015E90EAD981B155
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X69160 Genomic DNA. Translation: CAA48912.1.
    U00096 Genomic DNA. Translation: AAC74967.1.
    AP009048 Genomic DNA. Translation: BAA15718.1.
    PIRiI83401.
    RefSeqiNP_416411.1. NC_000913.3.
    WP_001295645.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74967; AAC74967; b1897.
    BAA15718; BAA15718; BAA15718.
    GeneIDi946406.
    KEGGiecj:JW1886.
    eco:b1897.
    PATRICi32119121. VBIEscCol129921_1978.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X69160 Genomic DNA. Translation: CAA48912.1.
    U00096 Genomic DNA. Translation: AAC74967.1.
    AP009048 Genomic DNA. Translation: BAA15718.1.
    PIRiI83401.
    RefSeqiNP_416411.1. NC_000913.3.
    WP_001295645.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP31678.
    SMRiP31678. Positions 18-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262243. 10 interactions.
    IntActiP31678. 15 interactions.
    STRINGi511145.b1897.

    2D gel databases

    SWISS-2DPAGEP31678.

    Proteomic databases

    PaxDbiP31678.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74967; AAC74967; b1897.
    BAA15718; BAA15718; BAA15718.
    GeneIDi946406.
    KEGGiecj:JW1886.
    eco:b1897.
    PATRICi32119121. VBIEscCol129921_1978.

    Organism-specific databases

    EchoBASEiEB1702.
    EcoGeneiEG11752. otsB.

    Phylogenomic databases

    eggNOGiENOG4108K4C. Bacteria.
    COG1877. LUCA.
    HOGENOMiHOG000239290.
    InParanoidiP31678.
    KOiK01087.
    OMAiWAMFLDI.
    OrthoDBiEOG6T7NBK.
    PhylomeDBiP31678.

    Enzyme and pathway databases

    UniPathwayiUPA00299.
    BioCyciEcoCyc:TREHALOSEPHOSPHASYN-MONOMER.
    ECOL316407:JW1886-MONOMER.
    MetaCyc:TREHALOSEPHOSPHASYN-MONOMER.

    Miscellaneous databases

    PROiP31678.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR003337. Trehalose_PPase.
    [Graphical view]
    PfamiPF02358. Trehalose_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    TIGR00685. T6PP. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "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: INDUCTION, NOMENCLATURE.
    6. "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.
    7. "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-PHOSPHATE PHOSPHATASE, INDUCTION.
    8. "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: INDUCTION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    9. "Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli."
      Weber A., Kogl S.A., Jung K.
      J. Bacteriol. 188:7165-7175(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family."
      Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V., Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.
      J. Biol. Chem. 281:36149-36161(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.

    Entry informationi

    Entry nameiOTSB_ECOLI
    AccessioniPrimary (citable) accession number: P31678
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: February 1, 1995
    Last modified: January 20, 2016
    This is version 118 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. 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.