ID   MTB2_BACIU              Reviewed;         360 AA.
AC   Q45489;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Type II methyltransferase M.BglII {ECO:0000303|PubMed:12654995};
DE            Short=M.BglII {ECO:0000303|PubMed:9073062};
DE            EC=2.1.1.113;
DE   AltName: Full=Modification methylase BglII;
DE   AltName: Full=N(4)- cytosine-specific methyltransferase BglII;
GN   Name=bglIIM {ECO:0000303|PubMed:9073062};
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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).
CC   -!- FUNCTION: A beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-AGATCT-3', methylates C-5 on both strands, and protects the
CC       DNA from cleavage by the BglII endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:9073062}.
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. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U49842; AAC45061.1; -; Genomic_DNA.
DR   PIR; JC6322; JC6322.
DR   AlphaFoldDB; Q45489; -.
DR   SMR; Q45489; -.
DR   REBASE; 156140; M.BsuHJ06ORF1941P.
DR   REBASE; 3304; M.BglII.
DR   BRENDA; 2.1.1.113; 658.
DR   PRO; PR:Q45489; -.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..360
FT                   /note="Type II methyltransferase M.BglII"
FT                   /id="PRO_0000087924"
FT   REGION          316..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   360 AA;  42043 MW;  B1C61DF49E5285D5 CRC64;
     MSEDQYKQIK LHLGMEDDNE DLPNHIPSSF PKQHLNKIYN GDTMNMLLDI PDNSVDLVVT
     SPPYNINKFK NDRRPLEEYL KWQTEIIEQC HRVLKPSGSI FWQVGTYVND SGAHIPLDIR
     FFPIFESLGM FPRNRIVWVR PHGLHANKKF AGRHETILWF TKTPEYKFFL DPIRVPQKYA
     NKKHYKGDKK GELSGDPLGK NPGDVWAFRN VRHNHEEDTI HPTQYPEDMI ERIVLSTTEP
     NDIVLDPFIG MGTTASVAKN LNRYFYGAEI EKEYVDIAYQ ILSGEPDENN NFPNLKTLRQ
     YCEKNGIIDP SQYTFTRQRK GSKPSLDSKA HPEEHHKKEI VERIEFEAEN SVYKKVQNEQ