ID T2B2_BACIU Reviewed; 223 AA. AC Q45488; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-MAY-2023, entry version 93. DE RecName: Full=Type II restriction enzyme BglII {ECO:0000303|PubMed:12654995}; DE Short=R.BglII; DE EC=3.1.21.4 {ECO:0000269|PubMed:10655616}; DE AltName: Full=Endonuclease BglII; DE AltName: Full=Type-2 restriction enzyme BglII; GN Name=bglIIR; OS Bacillus subtilis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Globigii / RUB562; RX PubMed=9073062; DOI=10.1016/s0378-1119(96)00638-5; RA Anton B.P., Heiter D.F., Benner J.S., Hess E.J., Greenough L., Moran L.S., RA Slatko B.E., Brooks J.E.; RT "Cloning and characterization of the BglII restriction-modification system RT reveals a possible evolutionary footprint."; RL Gene 187:19-27(1997). RN [2] RP NOMENCLATURE, AND SUBTYPE. RX PubMed=12654995; DOI=10.1093/nar/gkg274; RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K., RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S., RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A., RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S., RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V., RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E., RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W., RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.; RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing RT endonucleases and their genes."; RL Nucleic Acids Res. 31:1805-1812(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=10655616; DOI=10.1038/72405; RA Lukacs C.M., Kucera R., Schildkraut I., Aggarwal A.K.; RT "Understanding the immutability of restriction enzymes: crystal structure RT of BglII and its DNA substrate at 1.5 A resolution."; RL Nat. Struct. Biol. 7:134-140(2000). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-AGATCT-3' and cleaves after A-1. CC {ECO:0000269|PubMed:10655616, ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of DNA to give specific double- CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; CC Evidence={ECO:0000269|PubMed:10655616}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:10655616}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10655616}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49842; AAC45060.1; -; Genomic_DNA. DR PIR; JC6323; JC6323. DR PDB; 1D2I; X-ray; 1.70 A; A/B=1-223. DR PDB; 1DFM; X-ray; 1.50 A; A/B=1-223. DR PDB; 1ES8; X-ray; 2.30 A; A=1-223. DR PDBsum; 1D2I; -. DR PDBsum; 1DFM; -. DR PDBsum; 1ES8; -. DR AlphaFoldDB; Q45488; -. DR SMR; Q45488; -. DR BRENDA; 3.1.21.4; 658. DR EvolutionaryTrace; Q45488; -. DR PRO; PR:Q45488; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR CDD; cd22312; BglII-like; 1. DR Gene3D; 3.40.91.20; -; 1. DR InterPro; IPR011338; BamHI/BglII/BstY. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Restriction system. FT CHAIN 1..223 FT /note="Type II restriction enzyme BglII" FT /id="PRO_0000077286" FT BINDING 84 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT STRAND 2..8 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 17..29 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 50..61 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 74..79 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 100..115 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 126..132 FT /evidence="ECO:0007829|PDB:1DFM" FT HELIX 145..157 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 178..190 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 194..205 FT /evidence="ECO:0007829|PDB:1DFM" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:1DFM" SQ SEQUENCE 223 AA; 25763 MW; 4E71D916BABA7A45 CRC64; MKIDITDYNH ADEILNPQLW KEIEETLLKM PLHVKASDQA SKVGSLIFDP VGTNQYIKDE LVPKHWKNNI PIPKRFDFLG TDIDFGKRDT LVEVQFSNYP FLLNNTVRSE LFHKSNMDID EEGMKVAIII TKGHMFPASN SSLYYEQAQN QLNSLAEYNV FDVPIRLVGL IEDFETDIDI VSTTYADKRY SRTITKRDTV KGKVIDTNTP NTRRRKRGTI VTY //