T2B2_BACIU
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-AUG-2022, entry version 90.
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; Firmicutes; 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}.
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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 REBASE; 261; BglII.
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 Gene3D; 3.40.91.20; -; 1.
DR InterPro; IPR011338; BamHI/BglII/BstY.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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..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
