ID   MTBR_BACIU              Reviewed;         436 AA.
AC   P06530;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Type II methyltransferase M.BsuRI {ECO:0000303|PubMed:12654995};
DE            Short=M.BsuRI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase BsuRI;
DE   AltName: Full=Modification methylase BsuRI;
GN   Name=hsdRM; Synonyms=hsdM;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PROBABLE SUBUNIT, AND
RP   MUTAGENESIS OF 425-LEU--SER-436.
RC   STRAIN=R;
RX   PubMed=2997708; DOI=10.1093/nar/13.18.6403;
RA   Kiss A., Posfai G., Keller C.C., Venetianer P., Roberts R.J.;
RT   "Nucleotide sequence of the BsuRI restriction-modification system.";
RL   Nucleic Acids Res. 13:6403-6421(1985).
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 methylase, recognizes the double-stranded sequence 5'-GGCC-
CC       3', methylates C-3 on both strands, and protects the DNA from cleavage
CC       by the BsuRI endonuclease. {ECO:0000269|PubMed:2997708,
CC       ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:2997708}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; X02988; CAA26731.1; -; Genomic_DNA.
DR   PIR; B23488; XYBSR1.
DR   AlphaFoldDB; P06530; -.
DR   SMR; P06530; -.
DR   REBASE; 3340; M.BsuRI.
DR   PRO; PR:P06530; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..436
FT                   /note="Type II methyltransferase M.BsuRI"
FT                   /id="PRO_0000087864"
FT   DOMAIN          59..409
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
FT   MUTAGEN         425..436
FT                   /note="Missing: Retains methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:2997708"
SQ   SEQUENCE   436 AA;  49635 MW;  07EE0B2CA9140B19 CRC64;
     MTLKIDIKGR GKYKPASDYS IDDVKNVLME KIFEESSRII NSDDDLEIIE KVDFRTDKIN
     VLSLFSGCGG LDLGFELAGL AAVIGEQAAM EAFKDKDRFN ELRNKSIFHT IYTNDLFKEA
     NQTYKTNFPG HVIQHEKDIR QVKYFPKCNL ILGGFPCPGF SEAGPRLIDD DRNFLYLHFI
     RSLIQAQPEI FVAENVKGMM TLGKGEVLNQ IIEDFASAGY RVQFKLLNAR DYGVPQLRER
     VIIEGVRKDI SFNYKYPSPT HGEETGLKPF KTLRDSIGDL VTDPGPYFTG SYSSIYMSRN
     RKKSWDEQSF TIQASGRQAP LHPGGLSMKK IGKDKWVFPD GEENHRRLSV KEIARVQTFP
     DWFQFSQGTN SQTSINNRLD KQYKQIGNAV PVLLAKAVAS PIANWAINYL ESSPNNKIKN
     RERKLSIRTF LRIKTS