ID   MTB1_BACSQ              Reviewed;         912 AA.
AC   Q9LAI2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Type II beta methyltransferase M.BslI {ECO:0000303|PubMed:12654995};
DE            Short=M.BslI {ECO:0000303|PubMed:10648519};
DE            EC=2.1.1.113;
DE   AltName: Full=Modification methylase BslI;
DE   AltName: Full=N(4)- cytosine-specific methyltransferase BslI;
GN   Name=bslIM;
OS   Bacillus sp. (strain NEB-606).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=114630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP   1-MET--ILE-17.
RX   PubMed=10648519; DOI=10.1128/jb.182.4.949-955.2000;
RA   Hsieh P.-C., Xiao J.-P., O'Loane D., Xu S.-Y.;
RT   "Cloning, expression, and purification of a thermostable nonhomodimeric
RT   restriction enzyme, BslI.";
RL   J. Bacteriol. 182:949-955(2000).
RN   [2]
RP   NOMENCLATURE.
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 (PubMed:10648519). Recognizes the
CC       double-stranded sequence 5'-CCN(7)GG-3', methylates C-2 on both
CC       strands, and protects the DNA from cleavage by the BslI endonuclease
CC       (PubMed:12654995). {ECO:0000269|PubMed:10648519,
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. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF135191; AAF32529.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LAI2; -.
DR   SMR; Q9LAI2; -.
DR   REBASE; 3310; M.BslI.
DR   PRO; PR:Q9LAI2; -.
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   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..912
FT                   /note="Type II beta methyltransferase M.BslI"
FT                   /id="PRO_0000087922"
FT   MUTAGEN         1..17
FT                   /note="Missing: Partial loss of methylase activity."
FT                   /evidence="ECO:0000269|PubMed:10648519"
SQ   SEQUENCE   912 AA;  107439 MW;  8FFF7F1F86102C25 CRC64;
     MNWIFNTLIQ FLEDLNIDPS VVSLIDEDAK KLEEQFPKAL KHPVVDEEIV YKILCEKYNL
     NALNVKTISE TLNKEYKFGR NSKTALKKYL DYGKEEYLIQ FFNTLMLENN TYIDREYIES
     VLAFCEPVSK EKIKNEFIKL WNEANEVNEY GKLKDYLLGI YSKLFSMGLE NLRLIEIYNS
     NESLIKKVFK YESTIKELKE YCLSNQESIT AGLAIKMFNE KYMELMKKEY QQDAIALKLE
     EHMNQLYVDN NINEYPYIFD RGNDILLLPT EEYDFVYFHI DQDFFNRFQD ENKFLDYVLS
     SIKQIYRVLA NEKVFALKID NIYNNEKNLK WELYPKLTIY SEHFIQTKET ARFYKAYDIA
     KDLLSKHEFR LLENDSEKNR ENILKEYFSG KISEDELFSL VHVNMKKEHF FEFLNRFKYV
     HYGFTFNDCL VLDRVDKSFA NGELENVISN ATEILLIFYK FRADQRRIPC PSCGSLNISG
     NSYPEINNRS WECKSPYCPD RSKSNRGKRY SKKSNYMQWG AIYPKSHDII PRELIKKWRR
     DIIVINNEQE IFEMLVKYFS FTDEKLLFIN TNELPSVVTE RENRKVVILS QKLKEKAYTS
     NVVVKESLEG EIEFFKNGLY LKNFTELYLP EDQRRVSPEI NNFLNSGGRL KLIQGDSYEV
     LKSVEDNTFA AAVTSPPYYN AREYSQWPNL YLYFNDMYNI IKECFRTLKP GSVFLYNIAD
     IVDNENIIVK SSMGNKRIPL GAYTIYFFQK AGFELLDNII WDKGEPQSNR QKNDGKFTPH
     YQKPLNAYEH MFIFKKTGAP LTLSDDWQSK RGSWIKNIVP FQPVFKINSK GENILGHTAP
     FPEDIPRFVA NVFTKHDNDI ILDPFSGSLT SAIASYKSNR IGLGIELSPD YVELSRDRAL
     LEGVTTKILN FN