ID T2B1_BACIU Reviewed; 299 AA. AC O68557; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 03-MAY-2023, entry version 88. DE RecName: Full=Type II restriction enzyme BglI {ECO:0000303|PubMed:12654995}; DE Short=R.BglI; DE EC=3.1.21.4 {ECO:0000269|PubMed:9736624}; DE AltName: Full=Endonuclease BglI; DE AltName: Full=Type-2 restriction enzyme BglI; GN Name=bglIR; OS Bacillus subtilis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RC STRAIN=Globigii / RUB562; RX PubMed=9736624; DOI=10.1093/emboj/17.18.5466; RA Newman M., Lunnen K.D., Wilson G.G., Greci J., Schildkraut I., RA Philips S.E.V.; RT "Crystal structure of restriction endonuclease BglI bound to its RT interrupted DNA recognition sequence."; RL EMBO J. 17:5466-5476(1998). 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). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-GCCNNNNNGGC-3' and cleaves before N-8. CC {ECO:0000269|PubMed:9736624, 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:9736624}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 magnesium ions per subunit.; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9736624}. 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; AF050216; AAC63973.1; -; Genomic_DNA. DR PDB; 1DMU; X-ray; 2.20 A; A=1-299. DR PDBsum; 1DMU; -. DR AlphaFoldDB; O68557; -. DR SMR; O68557; -. DR EvolutionaryTrace; O68557; -. DR PRO; PR:O68557; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; cd22311; BglI-like; 1. DR Gene3D; 3.40.600.20; Restriction endonuclease BglI; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011543; Restrct_endonuc_II_BglI. DR InterPro; IPR043121; Restrct_endonuc_II_BglI_sf. DR Pfam; PF14562; Endonuc_BglI; 1. 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..299 FT /note="Type II restriction enzyme BglI" FT /id="PRO_0000077285" FT BINDING 116 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 116 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 142 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 143 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT TURN 2..5 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 6..22 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 24..44 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 46..58 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 83..89 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 91..99 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 116..122 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 124..129 FT /evidence="ECO:0007829|PDB:1DMU" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 135..143 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 206..220 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 230..240 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 243..247 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:1DMU" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 288..290 FT /evidence="ECO:0007829|PDB:1DMU" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:1DMU" SQ SEQUENCE 299 AA; 34014 MW; 40DF210E1173B02B CRC64; MYNLHREKIF MSYNQNKQYL EDNPEIQEKI ELYGLNLLNE VISDNEEEIR ADYNEANFLH PFWMNYPPLD RGKMPKGDQI PWIEVGEKAV GSKLTRLVSQ REDITVREIG LPTGPDERYL LTSPTIYSLT NGFTDSIMMF VDIKSVGPRD SDYDLVLSPN QVSGNGDWAQ LEGGIQNNQQ TIQGPRSSQI FLPTIPPLYI LSDGTIAPVV HLFIKPIYAM RSLTKGDTGQ SLYKIKLASV PNGLGLFCNP GYAFDSAYKF LFRPGKDDRT KSLLQKRVRV DLRVLDKIGP RVMTIDMDK //