ID   MTS9_STAAU              Reviewed;         430 AA.
AC   P23737;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Type II methyltransferase M.Sau96I {ECO:0000303|PubMed:12654995};
DE            Short=M.Sau96I {ECO:0000303|PubMed:2204026};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:2204026};
DE   AltName: Full=Cytosine-specific methyltransferase Sau96I;
DE   AltName: Full=Modification methylase Sau96I;
GN   Name=sau96IM {ECO:0000303|PubMed:2204026};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=PS96;
RX   PubMed=2204026; DOI=10.1093/nar/18.16.4659;
RA   Szilak L., Venetianer P., Kiss A.;
RT   "Cloning and nucleotide sequence of the genes coding for the Sau96I
RT   restriction and modification enzymes.";
RL   Nucleic Acids Res. 18:4659-4664(1990).
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       GGNCC-3', methylates C-4 on both strands, and protects the DNA from
CC       cleavage by the Sau96I endonuclease. {ECO:0000269|PubMed:2204026,
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         ECO:0000269|PubMed:2204026};
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; X53096; CAA37260.1; -; Genomic_DNA.
DR   PIR; S12705; S12705.
DR   AlphaFoldDB; P23737; -.
DR   SMR; P23737; -.
DR   REBASE; 182835; M.Bli37ORF2575P.
DR   REBASE; 182836; M.Bli14ORF1492P.
DR   REBASE; 182841; M.Bli34ORF1606P.
DR   REBASE; 195420; M.BliB11ORF1170P.
DR   REBASE; 204712; M.Bso1395ORF4807P.
DR   REBASE; 3496; M.Sau96I.
DR   PRIDE; P23737; -.
DR   PATRIC; fig|1280.3540.peg.2442; -.
DR   PRO; PR:P23737; -.
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; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
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; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
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; PS50943; HTH_CROC1; 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; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..430
FT                   /note="Type II methyltransferase M.Sau96I"
FT                   /id="PRO_0000087908"
FT   DOMAIN          9..63
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DOMAIN          99..429
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   430 AA;  49284 MW;  884FBD96F4890651 CRC64;
     MRLNKGSIIE KMKNQNIKTQ TELAEKIDIS KSQLSFMFSD EYEPLKKNVI KLADVLKVSP
     NDIILDEEDQ MPINSDFNRY DYKLDEFIDV SNVRKNKDYN VFETFAGAGG LALGLESAGL
     STYGAVEIDK NAAETLRINR PKWKVIENDI EFIADNLDEF IDEEIDILSG GYPCQTFSYA
     GKRNGFADTR GTLFYPYSKI LSKLKPKAFI AENVRGLVNH DDGKTLEVML KVFIKEGYEV
     YWNILNSWNY DVAQKRERIV IIGIREDLVK EQKYPFRFPL AQVYKPVLKD VLKDVPKSKV
     TAYSDKKREV MKLVPPGGCW VDLPEQIAKD YMGKSWYSGG GKRGMARRIS WDEPCLTLTT
     SPSQKQTERC HPDETRPFSI REYARIQSFP DEWEFSGGVG AQYRQIGNAV PVNLAKYIGK
     SLVHYLNQFN