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P04547

- GSTB_BPT4

UniProt

P04547 - GSTB_BPT4

Protein

DNA beta-glucosyltransferase

Gene

bgt

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. Is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system.1 Publication

    Catalytic activityi

    Transfers a beta-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA.

    Pathwayi

    GO - Molecular functioni

    1. DNA beta-glucosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. DNA modification Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Host-virus interaction, Restriction-modification system evasion by virus

    Enzyme and pathway databases

    UniPathwayiUPA00198.

    Protein family/group databases

    CAZyiGT63. Glycosyltransferase Family 63.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA beta-glucosyltransferase (EC:2.4.1.27)
    Short name:
    BGT
    Short name:
    Beta-GT
    Gene namesi
    Name:bgt
    OrganismiEnterobacteria phage T4 (Bacteriophage T4)
    Taxonomic identifieri10665 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
    Virus hostiEscherichia coli [TaxID: 562]
    ProteomesiUP000009087: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351DNA beta-glucosyltransferasePRO_0000164942Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Beta strandi14 – 174
    Helixi18 – 3215
    Beta strandi37 – 437
    Beta strandi46 – 505
    Helixi51 – 533
    Helixi56 – 583
    Beta strandi60 – 656
    Beta strandi73 – 753
    Helixi78 – 8912
    Beta strandi94 – 985
    Helixi109 – 1124
    Helixi118 – 1203
    Helixi123 – 1264
    Beta strandi132 – 1376
    Helixi142 – 1476
    Turni148 – 1503
    Beta strandi152 – 1598
    Helixi162 – 1643
    Helixi165 – 1684
    Beta strandi169 – 1713
    Beta strandi182 – 1876
    Helixi191 – 1933
    Helixi196 – 2038
    Beta strandi210 – 2156
    Helixi218 – 2203
    Beta strandi233 – 2353
    Helixi240 – 2423
    Helixi243 – 2475
    Beta strandi250 – 2556
    Helixi259 – 2613
    Turni262 – 2643
    Helixi268 – 2747
    Beta strandi276 – 2838
    Helixi284 – 2863
    Helixi296 – 2983
    Beta strandi299 – 3024
    Helixi303 – 31513
    Helixi317 – 33519
    Helixi338 – 34811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BGTX-ray2.20A1-351[»]
    1BGUX-ray2.20A1-351[»]
    1C3JX-ray1.88A1-351[»]
    1IXYX-ray2.50A/B1-351[»]
    1J39X-ray1.87A1-351[»]
    1JEJX-ray2.50A1-351[»]
    1JG6X-ray1.90A1-351[»]
    1JG7X-ray1.65A1-351[»]
    1JIUX-ray2.50A1-351[»]
    1JIVX-ray2.07A1-351[»]
    1JIXX-ray1.65A1-351[»]
    1M5RX-ray1.80A/B1-351[»]
    1NVKX-ray1.80A1-351[»]
    1NZDX-ray2.00A1-351[»]
    1NZFX-ray2.10A1-351[»]
    1QKJX-ray2.30A1-351[»]
    1SXPX-ray2.50A/B1-351[»]
    1SXQX-ray1.80A/B1-351[»]
    2BGTX-ray2.20A1-351[»]
    2BGUX-ray2.20A1-351[»]
    ProteinModelPortaliP04547.
    SMRiP04547. Positions 1-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04547.

    Family & Domainsi

    Family and domain databases

    InterProiIPR015281. Phage_T4_Bgt.
    [Graphical view]
    PfamiPF09198. T4-Gluco-transf. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04547-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIAIINMGN NVINFKTVPS SETIYLFKVI SEMGLNVDII SLKNGVYTKS    50
    FDEVDVNDYD RLIVVNSSIN FFGGKPNLAI LSAQKFMAKY KSKIYYLFTD 100
    IRLPFSQSWP NVKNRPWAYL YTEEELLIKS PIKVISQGIN LDIAKAAHKK 150
    VDNVIEFEYF PIEQYKIHMN DFQLSKPTKK TLDVIYGGSF RSGQRESKMV 200
    EFLFDTGLNI EFFGNAREKQ FKNPKYPWTK APVFTGKIPM NMVSEKNSQA 250
    IAALIIGDKN YNDNFITLRV WETMASDAVM LIDEEFDTKH RIINDARFYV 300
    NNRAELIDRV NELKHSDVLR KEMLSIQHDI LNKTRAKKAE WQDAFKKAID 350
    L 351
    Length:351
    Mass (Da):40,666
    Last modified:August 13, 1987 - v1
    Checksum:iD1F42B5FE6CB9D61
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti85 – 884KFMA → NLWQ in AAA88469. (PubMed:2832395)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03139 Genomic DNA. Translation: CAA26908.1.
    AF158101 Genomic DNA. Translation: AAD42545.1.
    M22767 Genomic DNA. Translation: AAA88469.1.
    M69268 Genomic DNA. Translation: AAA32544.1.
    Y00148 Genomic DNA. Translation: CAA68343.1.
    PIRiA00576. XUBPB4.
    RefSeqiNP_049658.1. NC_000866.4.

    Genome annotation databases

    GeneIDi1258765.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03139 Genomic DNA. Translation: CAA26908.1 .
    AF158101 Genomic DNA. Translation: AAD42545.1 .
    M22767 Genomic DNA. Translation: AAA88469.1 .
    M69268 Genomic DNA. Translation: AAA32544.1 .
    Y00148 Genomic DNA. Translation: CAA68343.1 .
    PIRi A00576. XUBPB4.
    RefSeqi NP_049658.1. NC_000866.4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BGT X-ray 2.20 A 1-351 [» ]
    1BGU X-ray 2.20 A 1-351 [» ]
    1C3J X-ray 1.88 A 1-351 [» ]
    1IXY X-ray 2.50 A/B 1-351 [» ]
    1J39 X-ray 1.87 A 1-351 [» ]
    1JEJ X-ray 2.50 A 1-351 [» ]
    1JG6 X-ray 1.90 A 1-351 [» ]
    1JG7 X-ray 1.65 A 1-351 [» ]
    1JIU X-ray 2.50 A 1-351 [» ]
    1JIV X-ray 2.07 A 1-351 [» ]
    1JIX X-ray 1.65 A 1-351 [» ]
    1M5R X-ray 1.80 A/B 1-351 [» ]
    1NVK X-ray 1.80 A 1-351 [» ]
    1NZD X-ray 2.00 A 1-351 [» ]
    1NZF X-ray 2.10 A 1-351 [» ]
    1QKJ X-ray 2.30 A 1-351 [» ]
    1SXP X-ray 2.50 A/B 1-351 [» ]
    1SXQ X-ray 1.80 A/B 1-351 [» ]
    2BGT X-ray 2.20 A 1-351 [» ]
    2BGU X-ray 2.20 A 1-351 [» ]
    ProteinModelPortali P04547.
    SMRi P04547. Positions 1-351.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT63. Glycosyltransferase Family 63.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1258765.

    Enzyme and pathway databases

    UniPathwayi UPA00198 .

    Miscellaneous databases

    EvolutionaryTracei P04547.

    Family and domain databases

    InterProi IPR015281. Phage_T4_Bgt.
    [Graphical view ]
    Pfami PF09198. T4-Gluco-transf. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "T4-induced alpha- and beta-glucosyltransferase: cloning of the genes and a comparison of their products based on sequencing data."
      Tomaschewski J., Gram H., Crabb J.W., Rueger W.
      Nucleic Acids Res. 13:7551-7568(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Expression and DNA sequence of the cloned bacteriophage T4 dCMP hydroxymethylase gene."
      Thylen C.
      J. Bacteriol. 170:1994-1998(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
    4. "Nucleotide sequence of the deoxycytidylate hydroxymethylase gene of bacteriophage T4 (g42) and the homology of its gene product with thymidylate synthase of E. coli."
      Lamm N., Tomaschewski J., Rueger W.
      Nucleic Acids Res. 15:3920-3920(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
    5. "Identification of a family of bacteriophage T4 genes encoding proteins similar to those present in group I introns of fungi and phage."
      Sharma M., Ellis R.L., Hinton D.M.
      Proc. Natl. Acad. Sci. U.S.A. 89:6658-6662(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-351.
    6. "Biochemical characterization of recombinant beta-glucosyltransferase and analysis of global 5-hydroxymethylcytosine in unique genomes."
      Terragni J., Bitinaite J., Zheng Y., Pradhan S.
      Biochemistry 51:1009-1019(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose."
      Vrelink A., Rueger W., Driessen H.P.C., Freemont P.S.
      EMBO J. 13:3413-3422(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    8. "T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism."
      Morera S., Imberty A., Aschke-Sonnenborn U., Ruger W., Freemont P.S.
      J. Mol. Biol. 292:717-730(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiGSTB_BPT4
    AccessioniPrimary (citable) accession number: P04547
    Secondary accession number(s): Q38417
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3