ID   MTB1_BACIU              Reviewed;         348 AA.
AC   O68556;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Type II methyltransferase M.BglI {ECO:0000303|PubMed:12654995};
DE            Short=M.BglI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.113;
DE   AltName: Full=BglI modification methyltransferase;
DE   AltName: Full=Modification methylase BglI;
DE   AltName: Full=N(4)- cytosine-specific methyltransferase BglI;
GN   Name=bglIM;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-GCCNNNNNGGC-3', methylates C-2 on both strands, and
CC       protects the DNA from cleavage by the BglI endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF050216; AAC63974.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68556; -.
DR   SMR; O68556; -.
DR   REBASE; 290972; M.Msa27082ORF4227P.
DR   REBASE; 3303; M.BglI.
DR   BRENDA; 2.1.1.113; 658.
DR   PRO; PR:O68556; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF08279; HTH_11; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..348
FT                   /note="Type II methyltransferase M.BglI"
FT                   /id="PRO_0000087923"
SQ   SEQUENCE   348 AA;  40242 MW;  7B08004E0DB7E707 CRC64;
     MNNHSYLKKN SFHEGDAREL LKCIEEESIA LSVWSPPYHV GKKYEEGQTY EQWSSLLTKV
     IALHYPILKP GGFLVINIDD ILAFPDPRMP RFQAVNLKKH RVSVTREDIL NALKLEPELT
     KYQLAKKFNC SEQTIERRLK GNNIRGGKYN VQTKVKLAGP VLEKAAEEAG LYLYDRRIWA
     KDPAWQNSQW HSNSYKAVSE FEHLYIFWKP GETVIDRNKL SKEEWASWAS RGIWYIPSVR
     KNDDHEAKFP LLLPQRLIKL LTQKGDTVLD CFMGSGTTAV AALSESRNFI GIEKEPKYIQ
     LSNKNVETFY ISRNKEASKI KETNHSVTDE KKKAEQLELL LEENENSL