ID GSTB_BPT4 Reviewed; 351 AA. AC P04547; Q38417; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=DNA beta-glucosyltransferase; DE Short=BGT; DE Short=Beta-GT; DE EC=2.4.1.27 {ECO:0000269|PubMed:6078540}; GN Name=bgt; OS Enterobacteria phage T4 (Bacteriophage T4). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Straboviridae; Tevenvirinae; Tequatrovirus. OX NCBI_TaxID=10665; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2999696; DOI=10.1093/nar/13.21.7551; RA Tomaschewski J., Gram H., Crabb J.W., Rueger W.; RT "T4-induced alpha- and beta-glucosyltransferase: cloning of the genes and a RT comparison of their products based on sequencing data."; RL Nucleic Acids Res. 13:7551-7568(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003; RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.; RT "Bacteriophage T4 genome."; RL Microbiol. Mol. Biol. Rev. 67:86-156(2003). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88. RX PubMed=2832395; DOI=10.1128/jb.170.4.1994-1998.1988; RA Thylen C.; RT "Expression and DNA sequence of the cloned bacteriophage T4 dCMP RT hydroxymethylase gene."; RL J. Bacteriol. 170:1994-1998(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. RX PubMed=3295783; DOI=10.1093/nar/15.9.3920; RA Lamm N., Tomaschewski J., Rueger W.; RT "Nucleotide sequence of the deoxycytidylate hydroxymethylase gene of RT bacteriophage T4 (g42) and the homology of its gene product with RT thymidylate synthase of E. coli."; RL Nucleic Acids Res. 15:3920-3920(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-351. RX PubMed=1631169; DOI=10.1073/pnas.89.14.6658; RA Sharma M., Ellis R.L., Hinton D.M.; RT "Identification of a family of bacteriophage T4 genes encoding proteins RT similar to those present in group I introns of fungi and phage."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6658-6662(1992). RN [6] RP CATALYTIC ACTIVITY. RX PubMed=6078540; DOI=10.1111/j.1432-1033.1967.tb00139.x; RA de Waard A., Ubbink T.E., Beukman W.; RT "On the specificity of bacteriophage-induced hydroxymethylcytosine RT glucosyltransferases. II. Specificities of hydroxymethylcytosine alphaand RT beta-glucosyltransferases induced by bacteriophage T4."; RL Eur. J. Biochem. 2:303-308(1967). RN [7] RP FUNCTION. RX PubMed=22229759; DOI=10.1021/bi2014739; RA Terragni J., Bitinaite J., Zheng Y., Pradhan S.; RT "Biochemical characterization of recombinant beta-glucosyltransferase and RT analysis of global 5-hydroxymethylcytosine in unique genomes."; RL Biochemistry 51:1009-1019(2012). RN [8] RP FUNCTION. RX PubMed=26081634; DOI=10.1128/mbio.00648-15; RA Bryson A.L., Hwang Y., Sherrill-Mix S., Wu G.D., Lewis J.D., Black L., RA Clark T.A., Bushman F.D.; RT "Covalent Modification of Bacteriophage T4 DNA Inhibits CRISPR-Cas9."; RL MBio 6:E00648-E00648(2015). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=8062817; DOI=10.1002/j.1460-2075.1994.tb06646.x; RA Vrelink A., Rueger W., Driessen H.P.C., Freemont P.S.; RT "Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in RT the presence and absence of the substrate uridine diphosphoglucose."; RL EMBO J. 13:3413-3422(1994). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10497034; DOI=10.1006/jmbi.1999.3094; RA Morera S., Imberty A., Aschke-Sonnenborn U., Ruger W., Freemont P.S.; RT "T4 phage beta-glucosyltransferase: substrate binding and proposed RT catalytic mechanism."; RL J. Mol. Biol. 292:717-730(1999). CC -!- FUNCTION: Catalyzes the transfer of glucose from uridine CC diphosphoglucose to 5-hydroxymethyl cytosine of T4 DNA to yield CC glucosyl 5-hydroxymethyl cytosine (glc-HMC) (PubMed:22229759). This DNA CC process seems to occur immediately after DNA synthesis since the DNA CC alpha-glucosyltransferase interacts with the clamp protein gp45 CC (PubMed:22229759). The glc-HMC modification protects the phage genome CC against its own nucleases and the host restriction endonuclease system CC (PubMed:22229759). The glc-HMC modification also protects against the CC host CRISPR-Cas9 defense system (PubMed:26081634). CC {ECO:0000269|PubMed:22229759, ECO:0000269|PubMed:26081634}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Transfers a beta-D-glucosyl residue from UDP-alpha-D-glucose CC to a hydroxymethylcytosine residue in DNA.; EC=2.4.1.27; CC Evidence={ECO:0000269|PubMed:6078540}; CC -!- PATHWAY: Genetic information processing; DNA modification. CC -!- SUBUNIT: Monomer. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03139; CAA26908.1; -; Genomic_DNA. DR EMBL; AF158101; AAD42545.1; -; Genomic_DNA. DR EMBL; AH003347; AAA88469.1; -; Genomic_DNA. DR EMBL; M69268; AAA32544.1; -; Genomic_DNA. DR EMBL; Y00148; CAA68343.1; -; Genomic_DNA. DR PIR; A00576; XUBPB4. DR RefSeq; NP_049658.1; NC_000866.4. DR PDB; 1BGT; X-ray; 2.20 A; A=1-351. DR PDB; 1BGU; X-ray; 2.20 A; A=1-351. DR PDB; 1C3J; X-ray; 1.88 A; A=1-351. DR PDB; 1IXY; X-ray; 2.50 A; A/B=1-351. DR PDB; 1J39; X-ray; 1.87 A; A=1-351. DR PDB; 1JEJ; X-ray; 2.50 A; A=1-351. DR PDB; 1JG6; X-ray; 1.90 A; A=1-351. DR PDB; 1JG7; X-ray; 1.65 A; A=1-351. DR PDB; 1JIU; X-ray; 2.50 A; A=1-351. DR PDB; 1JIV; X-ray; 2.07 A; A=1-351. DR PDB; 1JIX; X-ray; 1.65 A; A=1-351. DR PDB; 1M5R; X-ray; 1.80 A; A/B=1-351. DR PDB; 1NVK; X-ray; 1.80 A; A=1-351. DR PDB; 1NZD; X-ray; 2.00 A; A=1-351. DR PDB; 1NZF; X-ray; 2.10 A; A=1-351. DR PDB; 1QKJ; X-ray; 2.30 A; A=1-351. DR PDB; 1SXP; X-ray; 2.50 A; A/B=1-351. DR PDB; 1SXQ; X-ray; 1.80 A; A/B=1-351. DR PDB; 2BGT; X-ray; 2.20 A; A=1-351. DR PDB; 2BGU; X-ray; 2.20 A; A=1-351. DR PDBsum; 1BGT; -. DR PDBsum; 1BGU; -. DR PDBsum; 1C3J; -. DR PDBsum; 1IXY; -. DR PDBsum; 1J39; -. DR PDBsum; 1JEJ; -. DR PDBsum; 1JG6; -. DR PDBsum; 1JG7; -. DR PDBsum; 1JIU; -. DR PDBsum; 1JIV; -. DR PDBsum; 1JIX; -. DR PDBsum; 1M5R; -. DR PDBsum; 1NVK; -. DR PDBsum; 1NZD; -. DR PDBsum; 1NZF; -. DR PDBsum; 1QKJ; -. DR PDBsum; 1SXP; -. DR PDBsum; 1SXQ; -. DR PDBsum; 2BGT; -. DR PDBsum; 2BGU; -. DR SMR; P04547; -. DR DrugBank; DB01861; Uridine diphosphate glucose. DR DrugBank; DB03435; Uridine-5'-Diphosphate. DR CAZy; GT63; Glycosyltransferase Family 63. DR GeneID; 1258765; -. DR KEGG; vg:1258765; -. DR OrthoDB; 4125at10239; -. DR BRENDA; 2.4.1.27; 732. DR UniPathway; UPA00198; -. DR EvolutionaryTrace; P04547; -. DR Proteomes; UP000009087; Segment. DR GO; GO:0033821; F:DNA beta-glucosyltransferase activity; IDA:UniProtKB. DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-UniPathway. DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR015281; Phage_Bgt. DR Pfam; PF09198; T4-Gluco-transf; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 1: Evidence at protein level; KW 3D-structure; Glycosyltransferase; Host-virus interaction; KW Inhibition of host innate immune response by virus; Reference proteome; KW Restriction-modification system evasion by virus; Transferase; KW Viral immunoevasion. FT CHAIN 1..351 FT /note="DNA beta-glucosyltransferase" FT /id="PRO_0000164942" FT CONFLICT 85..88 FT /note="KFMA -> NLWQ (in Ref. 3; AAA88469)" FT /evidence="ECO:0000305" FT STRAND 3..10 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 18..32 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:1JIX" FT HELIX 78..89 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 109..112 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 123..126 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 142..147 FT /evidence="ECO:0007829|PDB:1JG7" FT TURN 148..150 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 152..159 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1SXP" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 196..203 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:1JIX" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 243..247 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:1JG7" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 268..274 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 276..283 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:1JG7" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:1JIX" FT HELIX 303..315 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 317..335 FT /evidence="ECO:0007829|PDB:1JG7" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:1JG7" SQ SEQUENCE 351 AA; 40666 MW; D1F42B5FE6CB9D61 CRC64; MKIAIINMGN NVINFKTVPS SETIYLFKVI SEMGLNVDII SLKNGVYTKS FDEVDVNDYD RLIVVNSSIN FFGGKPNLAI LSAQKFMAKY KSKIYYLFTD IRLPFSQSWP NVKNRPWAYL YTEEELLIKS PIKVISQGIN LDIAKAAHKK VDNVIEFEYF PIEQYKIHMN DFQLSKPTKK TLDVIYGGSF RSGQRESKMV EFLFDTGLNI EFFGNAREKQ FKNPKYPWTK APVFTGKIPM NMVSEKNSQA IAALIIGDKN YNDNFITLRV WETMASDAVM LIDEEFDTKH RIINDARFYV NNRAELIDRV NELKHSDVLR KEMLSIQHDI LNKTRAKKAE WQDAFKKAID L //