P04547 (GSTB_BPT4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA beta-glucosyltransferase
Short name=BGT
Short name=Beta-GT
EC=2.4.1.27

Gene names

Name:

bgt

Organism

Enterobacteria phage T4 (Bacteriophage T4) [Reference proteome]

Taxonomic identifier

10665 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus › Enterobacteria phage T4 sensu lato

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	Transfers a beta-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA.
Pathway	Genetic information processing; DNA modification.
Subunit structure	Monomer.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA modification Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	DNA beta-glucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 351

351

DNA beta-glucosyltransferase

PRO_0000164942

Experimental info

Sequence conflict

85 – 88

4

KFMA → NLWQ in AAA88469. Ref.3

Secondary structure

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351

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

14 – 17

4

Helix

18 – 32

15

Beta strand

37 – 43

7

Beta strand

46 – 50

5

Helix

51 – 53

3

Helix

56 – 58

3

Beta strand

60 – 65

6

Beta strand

73 – 75

3

Helix

78 – 89

12

Beta strand

94 – 98

5

Helix

109 – 112

4

Helix

118 – 120

3

Helix

123 – 126

4

Beta strand

132 – 137

6

Helix

142 – 147

6

Turn

148 – 150

3

Beta strand

152 – 159

8

Helix

162 – 164

3

Helix

165 – 168

4

Beta strand

169 – 171

3

Beta strand

182 – 187

6

Helix

191 – 193

3

Helix

196 – 203

8

Beta strand

210 – 215

6

Helix

218 – 220

3

Beta strand

233 – 235

3

Helix

240 – 242

3

Helix

243 – 247

5

Beta strand

250 – 255

6

Helix

259 – 261

3

Turn

262 – 264

3

Helix

268 – 274

7

Beta strand

276 – 283

8

Helix

284 – 286

3

Helix

296 – 298

3

Beta strand

299 – 302

4

Helix

303 – 315

13

Helix

317 – 335

19

Helix

338 – 348

11

Sequences

	Sequence		Length	Mass (Da)
	P04547 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: D1F42B5FE6CB9D61	FASTA	351	40,666
	10 20 30 40 50 60 MKIAIINMGN NVINFKTVPS SETIYLFKVI SEMGLNVDII SLKNGVYTKS FDEVDVNDYD 70 80 90 100 110 120 RLIVVNSSIN FFGGKPNLAI LSAQKFMAKY KSKIYYLFTD IRLPFSQSWP NVKNRPWAYL 130 140 150 160 170 180 YTEEELLIKS PIKVISQGIN LDIAKAAHKK VDNVIEFEYF PIEQYKIHMN DFQLSKPTKK 190 200 210 220 230 240 TLDVIYGGSF RSGQRESKMV EFLFDTGLNI EFFGNAREKQ FKNPKYPWTK APVFTGKIPM 250 260 270 280 290 300 NMVSEKNSQA IAALIIGDKN YNDNFITLRV WETMASDAVM LIDEEFDTKH RIINDARFYV 310 320 330 340 350 NNRAELIDRV NELKHSDVLR KEMLSIQHDI LNKTRAKKAE WQDAFKKAID L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Bacteriophage T4 genome." Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W. Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract] 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]	"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).
[7]	"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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

XUBPB4. A00576.

RefSeq

NP_049658.1. NC_000866.4.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P04547.

SMR

P04547. Positions 1-351.

ModBase

Search...

Protein family/group databases

CAZy

GT63. Glycosyltransferase Family 63.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1258765.

Enzyme and pathway databases

UniPathway

UPA00198.

Family and domain databases

InterPro

IPR015281. Phage_T4_Bgt.
[Graphical view]

Pfam

PF09198. T4-Gluco-transf. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04547.

Entry information

Entry name

GSTB_BPT4

Accession

Primary (citable) accession number: P04547
Secondary accession number(s): Q38417

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program