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Q45488

- T2B2_BACIU

UniProt

Q45488 - T2B2_BACIU

Protein

Type-2 restriction enzyme BglII

Gene

bglIIR

Organism
Bacillus subtilis
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (16 Apr 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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

    MKIDITDYNH ADEILNPQLW KEIEETLLKM PLHVKASDQA SKVGSLIFDP    50
    VGTNQYIKDE LVPKHWKNNI PIPKRFDFLG TDIDFGKRDT LVEVQFSNYP 100
    FLLNNTVRSE LFHKSNMDID EEGMKVAIII TKGHMFPASN SSLYYEQAQN 150
    QLNSLAEYNV FDVPIRLVGL IEDFETDIDI VSTTYADKRY SRTITKRDTV 200
    KGKVIDTNTP NTRRRKRGTI VTY 223
    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