T2B1_BACIU
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-AUG-2022, entry version 85.
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; Firmicutes; 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}.
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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 REBASE; 260; BglI.
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 Gene3D; 3.40.600.20; -; 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; SSF52980; 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
