Reviewed, UniProtKB/Swiss-Prot O68557 (T2B1_BACSU)

Names and origin

Protein names

Recommended name:
    Type-2 restriction enzyme BglI
      Short name=R.BglI
    EC=3.1.21.4
Alternative name(s):
    Type II restriction enzyme BglI
    Endonuclease BglI

Gene names

Name:

bglIR

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes the double-stranded sequence GCCNNNNNGGC and cleaves before N-8.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Binds 2 magnesium ions per subunit.

Ontologies

Keywords
Biological process	Restriction system
Ligand	Magnesium Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro Type II site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

Type-2 restriction enzyme BglI

PRO_0000077285

Sites

Metal binding

116

1

Magnesium 1

Metal binding

116

1

Magnesium 2

Metal binding

142

1

Magnesium 1

Metal binding

143

1

Magnesium 1; via carbonyl oxygen

Secondary structure

1

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299

Helix Strand Turn

Details...

Turn

2 – 5

4

Helix

6 – 22

17

Helix

24 – 44

21

Helix

46 – 58

13

Helix

60 – 63

4

Beta strand

72 – 74

3

Helix

83 – 89

7

Helix

91 – 99

9

Beta strand

105 – 107

3

Beta strand

116 – 122

7

Helix

124 – 129

6

Turn

130 – 132

3

Beta strand

135 – 143

9

Beta strand

154 – 157

4

Helix

159 – 161

3

Beta strand

180 – 183

4

Beta strand

188 – 191

4

Beta strand

197 – 200

4

Beta strand

206 – 220

15

Helix

221 – 223

3

Beta strand

230 – 240

11

Helix

243 – 247

5

Helix

252 – 254

3

Helix

256 – 258

3

Beta strand

261 – 264

4

Beta strand

278 – 281

4

Helix

282 – 285

4

Beta strand

288 – 290

3

Beta strand

292 – 296

5

Sequences

	Sequence		Length	Mass (Da)
	O68557-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 40DF210E1173B02B	FASTA	299	34,014
	10 20 30 40 50 60 MYNLHREKIF MSYNQNKQYL EDNPEIQEKI ELYGLNLLNE VISDNEEEIR ADYNEANFLH 70 80 90 100 110 120 PFWMNYPPLD RGKMPKGDQI PWIEVGEKAV GSKLTRLVSQ REDITVREIG LPTGPDERYL 130 140 150 160 170 180 LTSPTIYSLT NGFTDSIMMF VDIKSVGPRD SDYDLVLSPN QVSGNGDWAQ LEGGIQNNQQ 190 200 210 220 230 240 TIQGPRSSQI FLPTIPPLYI LSDGTIAPVV HLFIKPIYAM RSLTKGDTGQ SLYKIKLASV 250 260 270 280 290 PNGLGLFCNP GYAFDSAYKF LFRPGKDDRT KSLLQKRVRV DLRVLDKIGP RVMTIDMDK

References

[1]

"Crystal structure of restriction endonuclease BGlI bound to its interrupted DNA recognition sequence." Newman M., Lunnen K.D., Wilson G.G., Greci J., Schildkraut I., Philips S.E.V. EMBO J. 17:5466-5476(1998) [PubMed: 9736624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). Strain: Globigii / RUB562.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF050216 Genomic DNA. Translation: AAC63973.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DMU	X-ray	2.20	A	1-299	[»]

ModBase

Search...

Protein family/group databases

REBASE

260. BglI.

Enzyme and pathway databases

BRENDA

3.1.21.4. 150.

Family and domain databases

InterPro

IPR011543. Restrict_endonuc_II_BglI_core.
[Graphical view]

Gene3D

G3DSA:3.40.600.20. Restrict_endonuc_II_BglI_core. 1 hit.

ProtoNet

Search...

Entry information

Entry name

T2B1_BACSU

Accession

Primary (citable) accession number: O68557

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	August 1, 1998
Last modified:	May 5, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)