Reviewed, UniProtKB/Swiss-Prot Q45488 (T2B2_BACSU)

Names and origin

Protein names

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

Gene names

Name:

bglIIR

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	223 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 AGATCT and cleaves after A-1.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Homodimer.

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 – 223

223

Type-2 restriction enzyme BglII

PRO_0000077286

Sites

Metal binding

84

1

Magnesium

Metal binding

94

1

Magnesium; via carbonyl oxygen

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

223

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

11 – 14

4

Helix

17 – 29

13

Beta strand

32 – 36

5

Beta strand

46 – 48

3

Helix

50 – 61

12

Helix

62 – 64

3

Beta strand

67 – 71

5

Helix

74 – 79

6

Beta strand

81 – 87

7

Beta strand

90 – 94

5

Helix

100 – 114

15

Beta strand

118 – 123

6

Beta strand

126 – 132

7

Helix

145 – 157

13

Beta strand

165 – 171

7

Beta strand

178 – 190

13

Beta strand

194 – 205

12

Beta strand

219 – 222

4

Sequences

	Sequence		Length	Mass (Da)
	Q45488-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4E71D916BABA7A45	FASTA	223	25,763
	10 20 30 40 50 60 MKIDITDYNH ADEILNPQLW KEIEETLLKM PLHVKASDQA SKVGSLIFDP VGTNQYIKDE 70 80 90 100 110 120 LVPKHWKNNI PIPKRFDFLG TDIDFGKRDT LVEVQFSNYP FLLNNTVRSE LFHKSNMDID 130 140 150 160 170 180 EEGMKVAIII TKGHMFPASN SSLYYEQAQN QLNSLAEYNV FDVPIRLVGL IEDFETDIDI 190 200 210 220 VSTTYADKRY SRTITKRDTV KGKVIDTNTP NTRRRKRGTI VTY

References

[1]	"Cloning and characterization of the BglII restriction-modification system reveals a possible evolutionary footprint." Anton B.P., Heiter D.F., Benner J.S., Hess E.J., Greenough L., Moran L.S., Slatko B.E., Brooks J.E. Gene 187:19-27(1997) [PubMed: 9073062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Globigii / RUB562.
[2]	"Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 A resolution." Lukacs C.M., Kucera R., Schildkraut I., Aggarwal A.K. Nat. Struct. Biol. 7:134-140(2000) [PubMed: 10655616] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U49842 Genomic DNA. Translation: AAC45060.1.

PIR

JC6323.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2I	X-ray	1.70	A/B	1-223	[»]
1DFM	X-ray	1.50	A/B	1-223	[»]
1ES8	X-ray	2.30	A	1-223	[»]

ModBase

Search...

Protein family/group databases

REBASE

261. BglII.

Enzyme and pathway databases

BRENDA

3.1.21.4. 150.

Family and domain databases

InterPro

IPR011338. Restrct_endonuc_II_BamHI/BglII.
IPR015278. Restrict_endonuc_II_BglII.
[Graphical view]

Gene3D

G3DSA:3.40.91.20. Restrct_endonuc_II_BamHI/BglII. 1 hit.

Pfam

PF09195. Endonuc-BglII. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

T2B2_BACSU

Accession

Primary (citable) accession number: Q45488

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 50 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)