ID   T2BF_BACIU              Reviewed;         395 AA.
AC   P25217;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Type II restriction enzyme BsuFI {ECO:0000303|PubMed:12654995};
DE            Short=R.BsuFI {ECO:0000303|PubMed:1721700};
DE            EC=3.1.21.4 {ECO:0000269|PubMed:1721700};
DE   AltName: Full=Endonuclease BsuFI;
DE   AltName: Full=Type-2 restriction enzyme BsuFI;
GN   Name=hsdFR; Synonyms=hsrF;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, FUNCTION,
RP   CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ISF18;
RX   PubMed=1721700; DOI=10.1093/nar/19.23.6457;
RA   Kapfer W., Walter J., Trautner T.A.;
RT   "Cloning, characterization and evolution of the BsuFI restriction
RT   endonuclease gene of Bacillus subtilis and purification of the enzyme.";
RL   Nucleic Acids Res. 19:6457-6463(1991).
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'-CCGG-3' and cleaves after C-1.
CC       {ECO:0000269|PubMed:1721700, 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:1721700};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:1721700}.
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DR   EMBL; X62104; CAA44014.1; -; Genomic_DNA.
DR   PIR; S20059; S20059.
DR   AlphaFoldDB; P25217; -.
DR   SMR; P25217; -.
DR   REBASE; 203787; Bsu1444ORF756P.
DR   REBASE; 203790; Bsu757ORF755P.
DR   REBASE; 205273; Bsu761ORF757P.
DR   REBASE; 205286; Bsu333ORF764P.
DR   PRO; PR:P25217; -.
DR   GO; GO:0003677; F:DNA 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   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR015291; Restrct_endonuc_II_MspI.
DR   Pfam; PF09208; Endonuc-MspI; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW   Restriction system.
FT   CHAIN           1..395
FT                   /note="Type II restriction enzyme BsuFI"
FT                   /id="PRO_0000077291"
SQ   SEQUENCE   395 AA;  45540 MW;  C1E7D88FDAAC623D CRC64;
     MNKDNQIKNE SGKQAKILVS EIVNNLKNEL GINIEIEEGY SIGYPNQEKQ FKMDFLVQFT
     DFDNEQWLIK STNSIRERIY GTEFFAQNIR LIDEKVKNIY VVVPDSISSA EMKKKRNYSV
     KINGTTYTSF LTDVLTVNEL RQKIVEKASQ NIAQGLRANV LGNDAETSIV NLLNDLKNKA
     LWNDYQNAQQ TIKSSTYKIY KEILEKIDLK EGFDKILEVT ATNDIPLLSN RGKPKTDVSV
     TIKTNTKELI RNISIKNTRE KTVTIHEGSV SDLISRLKLS ETDPLSQALI HFEKVGSKKK
     LIAEHPNSDK ILEENLKLYN RELIEFLHSP LLNDKIQMVD LIIFTNKFAV WNRDDYIKHY
     IEEYSGKGQF GTPFKWTYPS KKRGQKIQIK GFSNN