ID   MTB1_LYSSH              Reviewed;         424 AA.
AC   P13906;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 3.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Type II methyltransferase M.BspRI {ECO:0000303|PubMed:12654995};
DE            Short=M.BspRI {ECO:0000303|PubMed:6313947};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase BspRI;
DE   AltName: Full=Modification methylase BspRI;
GN   Name=bspRIM;
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=R;
RX   PubMed=6313947; DOI=10.1016/s0022-2836(83)80123-5;
RA   Posfai G., Kiss A., Erdei S., Posfai J., Venetianer P.;
RT   "Structure of the Bacillus sphaericus R modification methylase gene.";
RL   J. Mol. Biol. 170:597-610(1983).
RN   [2]
RP   SEQUENCE REVISION TO 322, PARTIAL PROTEIN SEQUENCE, METHYLATION AT CYS-181,
RP   COVALENT METHYLCYSTEINYL INTERMEDIATE, AND ACTIVE SITE.
RX   PubMed=8065896; DOI=10.1093/nar/22.15.2876;
RA   Szilak L., Finta C., Patthy A., Venetianer P., Kiss A.;
RT   "Self-methylation of BspRI DNA-methyltransferase.";
RL   Nucleic Acids Res. 22:2876-2881(1994).
RN   [3]
RP   SEQUENCE REVISION TO 394.
RA   Rasko T., Der A., Klement E., Posfai E., Medzihradszky K.F., Marshak D.R.,
RA   Roberts R.J., Kiss A.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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 BspRI endonuclease. {ECO:0000269|PubMed:6313947,
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:6313947}.
CC   -!- PTM: In the absence of DNA, can self-methylate two cysteine residues.
CC       {ECO:0000269|PubMed:8065896}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15758; CAA33764.2; -; Genomic_DNA.
DR   PIR; S07792; S07792.
DR   AlphaFoldDB; P13906; -.
DR   SMR; P13906; -.
DR   REBASE; 3322; M.BspRI.
DR   iPTMnet; P13906; -.
DR   PRO; PR:P13906; -.
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; 2.
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   Direct protein sequencing; DNA-binding; Methylation; Methyltransferase;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..424
FT                   /note="Type II methyltransferase M.BspRI"
FT                   /id="PRO_0000087862"
FT   DOMAIN          58..408
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        156
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000269|PubMed:8065896"
FT   MOD_RES         181
FT                   /note="S-methylcysteine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:8065896"
SQ   SEQUENCE   424 AA;  48212 MW;  1DED6A45DB0A4FCF CRC64;
     MAIKINEKGR GKFKPAPTYE KEEVRQLLME KINEEMEAVA TATSDISNDE IQYKSDKFNV
     LSLFCGAGGL DLGFELAGLE QSLGTDKALE AFKDRDVYNA IRHESVFHTV YANDIFSEAL
     QTYEKNMPNH VFIHEKDIRK IKEFPSANLV IGGFPCPGFS EAGPRLVDDE RNFLYIHFIR
     CLMQVQPEIF VAENVKGMMT LGGGEVFRQI VEDFGAAGYR VEARLLNARD YGVPQIRERV
     IIVGVRNDID FNYEYPEITH GNEEGLKPYV TLEEAIGDLS LDPGPYFTGS YSTIFMSRNR
     KKKWTDQSFT IQASGRQAPI HPGGLPMEKV DKNKWIFPDG EENHRRLSVK EIKRIQTFPD
     WYEFSDGGNM KVSVNNRLDK QYKQIGNAVP VFLARAVAKS IAQFAADYLK DNHPHEAPQM
     KLFI