T2B1_GEOSE
ID T2B1_GEOSE Reviewed; 323 AA.
AC P70985;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Type II restriction enzyme BsoBI {ECO:0000303|PubMed:12654995};
DE Short=R.BsoBI;
DE EC=3.1.21.4;
DE AltName: Full=Endonuclease BsoBI;
DE AltName: Full=Type-2 restriction enzyme BsoBI;
GN Name=bsoBIR {ECO:0000303|PubMed:8917312};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-17, AND FUNCTION.
RC STRAIN=JN209;
RX PubMed=8917312; DOI=10.1007/bf02173975;
RA Ruan H., Lunnen K.D., Scott M.E., Moran L.S., Slatko B.E., Pelletier J.J.,
RA Hess E.J., Benner J. II, Wilson G.G., Xu S.-Y.;
RT "Cloning and sequence comparison of AvaI and BsoBI restriction-modification
RT systems.";
RL Mol. Gen. Genet. 252:695-699(1996).
RN [2]
RP FUNCTION, MUTAGENESIS OF ASP-212 AND ASP-246, AND DNA-BINDING.
RC STRAIN=JN209;
RX PubMed=9099856; DOI=10.1016/s0378-1119(96)00773-1;
RA Ruan H., Lunnen K.D., Pelletier J.J., Xu S.-Y.;
RT "Overexpression of BsoBI restriction endonuclease in E. coli, purification
RT of the recombinant BsoBI, and identification of catalytic residues of BsoBI
RT by random mutagenesis.";
RL Gene 188:35-39(1997).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT.
RX PubMed=11250198; DOI=10.1016/s0969-2126(01)00564-0;
RA van der Woerd M.J., Pelletier J.J., Xu S.-Y., Friedman A.M.;
RT "Restriction enzyme BsoBI-DNA complex: a tunnel for recognition of
RT degenerate DNA sequences and potential histidine catalysis.";
RL Structure 9:133-144(2001).
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded sequence 5'-CYCGRG-3' and cleaves after C-1.
CC {ECO:0000269|PubMed:9099856, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:8917312}.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11250198}.
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DR EMBL; X98287; CAA66932.1; -; Genomic_DNA.
DR PIR; S72473; S72473.
DR PDB; 1DC1; X-ray; 1.70 A; A/B=1-323.
DR PDBsum; 1DC1; -.
DR AlphaFoldDB; P70985; -.
DR SMR; P70985; -.
DR EvolutionaryTrace; P70985; -.
DR PRO; PR:P70985; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.10.238.90; -; 1.
DR InterPro; IPR043091; Restr_endonucII_AvaI/BsoBI_hel.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR015277; Restrct_endonuc_II_AvaI/BsoBI.
DR Pfam; PF09194; Endonuc-BsobI; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Restriction system.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8917312"
FT CHAIN 2..323
FT /note="Type II restriction enzyme BsoBI"
FT /id="PRO_0000077288"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT SITE 81
FT /note="Interaction with DNA"
FT SITE 131
FT /note="Interaction with DNA"
FT MUTAGEN 212
FT /note="D->N: Loss of activity, still binds DNA."
FT /evidence="ECO:0000269|PubMed:9099856"
FT MUTAGEN 246
FT /note="D->N: Loss of activity, still binds DNA."
FT /evidence="ECO:0000269|PubMed:9099856"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 21..53
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:1DC1"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 110..152
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:1DC1"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 247..270
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:1DC1"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:1DC1"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:1DC1"
SQ SEQUENCE 323 AA; 36706 MW; C5D71CA25DA95B27 CRC64;
MNTQKPFENH LKSVDDLKTT YEEYRAGFIA FALEKNKRST PYIERARALK VAASVAKTPK
DLLYLEDIQD ALLYASGISD KAKKFLTEDD KKESINNLIE NFLEPAGEEF IDELIFRYLL
FQGDSLGGTM RNIAGALAQQ KLTRAIISAL DIANIPYKWL DSRDKKYTNW MDKPEDDYEL
ETFAKGISWT INGKHRTLMY NITVPLVKKN VDICLFNCEP EIYTPQKVHQ QPEKYLLLGE
LKGGIDPAGA DEHWKTANTA LTRIRNKFSE KGLSPKTIFI GAAIEHSMAE EIWDQLQSGS
LTNSANLTKT EQVGSLCRWI INI
