ID   MTBB_BACIU              Reviewed;         501 AA.
AC   P33563;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Type II methyltransferase M.BsuBI {ECO:0000303|PubMed:12654995};
DE            Short=M.BsuBI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72 {ECO:0000269|PubMed:1480472};
DE   AltName: Full=Adenine-specific methyltransferase BsuBI;
DE   AltName: Full=Modification methylase BsuBI;
DE   AltName: Full=Type II methyltransferase BsuBI {ECO:0000303|PubMed:12654995};
GN   Name=hsdBM; Synonyms=hsmB;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ISB8;
RX   PubMed=1480472; DOI=10.1093/nar/20.24.6517;
RA   Xu G.-L., Kapfer W., Walter J., Trautner T.A.;
RT   "BsuBI -- an isospecific restriction and modification system of PstI:
RT   characterization of the BsuBI genes and enzymes.";
RL   Nucleic Acids Res. 20:6517-6523(1992).
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 that recognizes the double-stranded
CC       sequence 5'-CTGCAG-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the BsuBI endonuclease.
CC       {ECO:0000269|PubMed:1480472, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000269|PubMed:1480472};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; L01541; AAA18169.1; -; Genomic_DNA.
DR   PIR; S35515; S35515.
DR   AlphaFoldDB; P33563; -.
DR   REBASE; 203431; M.Bat1359ORF636P.
DR   REBASE; 3336; M.BsuBI.
DR   PRO; PR:P33563; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-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; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..501
FT                   /note="Type II methyltransferase M.BsuBI"
FT                   /id="PRO_0000087946"
SQ   SEQUENCE   501 AA;  57198 MW;  AC33B2944699653E CRC64;
     MTQILETVDK SRLTVNPLLK NKSELGQFFT PSSISIFMAC LFSEDKLNNA KVLDAGAGIG
     SLTSAFLARL ISENIGKADL HLLEIDEMLE PYLSETLALF KDYIEINSQI IIDDFIEWAA
     YSLLDEESLL AKDKQRFTHA ILNPPYKKIK SNSKHRKLLR KAGIETVNLY SAFVALTVDL
     MSDGGEIVFI IPRSFCNGPY FRHFRQHLLN KTSIKHMHLF ESRDKAFKDD EVLQENVISK
     LEKGTVQEDV KISISTDDSF SVIRSYRYPF EKIVQPNDIE KFIHINTTNE ETLIEKHPNV
     CYSLEELNIE VSTGPVVDFR VKENLREMPG EGTVPLFYPN HFVGTSLEYP KMMKKPNAII
     RNEKVEKWLY PNGHYVVVKR FSSKEEKRRI VAGVLTPESV NDPVVGFENG LNVLHYNKSG
     ISKEVAYGLY AYLNSTPVDK YFRIFNGHTQ VNATDLRTMK FPSRDILISL GKWVIENIEN
     VGQVEIDSKL EELLLNDRGN A