ID   MTB6_BACSF              Reviewed;         315 AA.
AC   P43420;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   13-SEP-2023, entry version 82.
DE   RecName: Full=Type II methyltransferase M.Bsp6I {ECO:0000303|PubMed:12654995};
DE            Short=M.Bsp6I {ECO:0000303|PubMed:7607501};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase Bsp6I;
DE   AltName: Full=Modification methylase Bsp6I;
GN   Name=bsp6IM {ECO:0000303|PubMed:7607501};
OS   Bacillus sp. (strain RFL6).
OG   Plasmid pXH13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=72577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=RFL6;
RX   PubMed=7607501; DOI=10.1016/0378-1119(94)00795-t;
RA   Lubys A., Janulaitis A.;
RT   "Cloning and analysis of the plasmid-borne genes encoding the Bsp6I
RT   restriction and modification enzymes.";
RL   Gene 157:25-29(1995).
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 that recognizes the double-stranded sequence 5'-
CC       GCNGC-3', methylates C-? on both strands, and protects the DNA from
CC       cleavage by the Bsp6I endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:7607501}.
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   -!- 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; X81638; CAA57293.1; -; Genomic_DNA.
DR   PIR; I40138; I40138.
DR   AlphaFoldDB; P43420; -.
DR   SMR; P43420; -.
DR   REBASE; 205334; M.Bso1395ORF1169P.
DR   REBASE; 3315; M.Bsp6I.
DR   PRO; PR:P43420; -.
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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..315
FT                   /note="Type II methyltransferase M.Bsp6I"
FT                   /id="PRO_0000087859"
FT   DOMAIN          2..315
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   315 AA;  36315 MW;  ED2DD748AD33E44F CRC64;
     MLQIASLFAG VGGIDLGFEQ TGYFETVWAN EYDKNAAITY QSNFKNKLII DDIRNIKVED
     VPDFDVLLSG FPCTSFSVAG YRKGFEDEKS GDLFFETLRL IVAKKPQVIF LENVKNLVGH
     DNGNTFKVIY EALESNGYHI KYQVLNAKDF GNIPQNRERI YIVGFRNIEH YKNFNFPMPQ
     PLTLTIKDMI NLSDKLDDRF YYTEDKCSFY SPLQEQMTSD ETIYQWRRKY VRENKSNVCP
     TLTANMGTGG HNVPLVKTKH GIRKLTPREC FNFQGYPEDF ILPELAPTHL YKQAGNSVVV
     PVIRRIAENI YKSML
//