GSTB_BPT4
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 03-AUG-2022, entry version 114.
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 Caudovirales; Myoviridae; 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.
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DR EMBL; X03139; CAA26908.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42545.1; -; Genomic_DNA.
DR EMBL; M22767; 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 BRENDA; 2.4.1.27; 732.
DR UniPathway; UPA00198; -.
DR EvolutionaryTrace; P04547; -.
DR Proteomes; UP000009087; Genome.
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 InterPro; IPR015281; Phage_Bgt.
DR Pfam; PF09198; T4-Gluco-transf; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Host-virus interaction;
KW Reference proteome; Restriction-modification system evasion by virus;
KW Transferase.
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
