Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q45488

- T2B2_BACIU

UniProt

Q45488 - T2B2_BACIU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Type-2 restriction enzyme BglII

Gene

bglIIR

Organism
Bacillus subtilis
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Recognizes the double-stranded sequence AGATCT and cleaves after A-1.

Catalytic activityi

Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Cofactori

Binds 1 magnesium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Magnesium
Metal bindingi94 – 941Magnesium; via carbonyl oxygen

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. magnesium ion binding Source: InterPro
  3. Type II site-specific deoxyribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Restriction system

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

REBASEi261. BglII.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 restriction enzyme BglII (EC:3.1.21.4)
Short name:
R.BglII
Alternative name(s):
Endonuclease BglII
Type II restriction enzyme BglII
Gene namesi
Name:bglIIR
OrganismiBacillus subtilis
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Type-2 restriction enzyme BglIIPRO_0000077286Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
223
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87
Helixi11 – 144
Helixi17 – 2913
Beta strandi32 – 365
Beta strandi46 – 483
Helixi50 – 6112
Helixi62 – 643
Beta strandi67 – 715
Helixi74 – 796
Beta strandi81 – 877
Beta strandi90 – 945
Helixi100 – 11516
Beta strandi118 – 1236
Beta strandi126 – 1327
Helixi145 – 15713
Beta strandi165 – 1717
Beta strandi178 – 19013
Beta strandi194 – 20512
Beta strandi219 – 2224

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2IX-ray1.70A/B1-223[»]
1DFMX-ray1.50A/B1-223[»]
1ES8X-ray2.30A1-223[»]
ProteinModelPortaliQ45488.
SMRiQ45488. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45488.

Family & Domainsi

Family and domain databases

Gene3Di3.40.91.20. 1 hit.
InterProiIPR011338. BamHI/BglII/BstY.
IPR011335. Restrct_endonuc-II-like.
IPR015278. Restrct_endonuc_II_BglII.
[Graphical view]
PfamiPF09195. Endonuc-BglII. 1 hit.
[Graphical view]
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

Q45488-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIDITDYNH ADEILNPQLW KEIEETLLKM PLHVKASDQA SKVGSLIFDP
60 70 80 90 100
VGTNQYIKDE LVPKHWKNNI PIPKRFDFLG TDIDFGKRDT LVEVQFSNYP
110 120 130 140 150
FLLNNTVRSE LFHKSNMDID EEGMKVAIII TKGHMFPASN SSLYYEQAQN
160 170 180 190 200
QLNSLAEYNV FDVPIRLVGL IEDFETDIDI VSTTYADKRY SRTITKRDTV
210 220
KGKVIDTNTP NTRRRKRGTI VTY
Length:223
Mass (Da):25,763
Last modified:November 1, 1996 - v1
Checksum:i4E71D916BABA7A45
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U49842 Genomic DNA. Translation: AAC45060.1.
PIRiJC6323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U49842 Genomic DNA. Translation: AAC45060.1 .
PIRi JC6323.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q45488.
SMRi Q45488. Positions 1-223.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 261. BglII.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q45488.

Family and domain databases

Gene3Di 3.40.91.20. 1 hit.
InterProi IPR011338. BamHI/BglII/BstY.
IPR011335. Restrct_endonuc-II-like.
IPR015278. Restrct_endonuc_II_BglII.
[Graphical view ]
Pfami PF09195. Endonuc-BglII. 1 hit.
[Graphical view ]
SUPFAMi SSF52980. SSF52980. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiT2B2_BACIU
AccessioniPrimary (citable) accession number: Q45488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries

External Data

Dasty 3