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Database: UniProt
Entry: P23737
LinkDB: P23737
Original site: P23737 
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   11-JUN-2014, entry version 89.
DE   RecName: Full=Modification methylase Sau96I;
DE            Short=M.Sau96I;
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase Sau96I;
GN   Name=sau96IM;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
CC   -!- FUNCTION: This methylase recognizes the double-stranded sequence
CC       GGNCC, causes specific methylation on C-4 on both strands, and
CC       protects the DNA from cleavage by the Sau96I endonuclease.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC       homocysteine + DNA containing 5-methylcytosine.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. C5-methyltransferase family.
CC   -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 SAM-dependent MTase C5-type domain.
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DR   EMBL; X53096; CAA37260.1; -; Genomic_DNA.
DR   PIR; S12705; S12705.
DR   ProteinModelPortal; P23737; -.
DR   REBASE; 3496; M.Sau96I.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   PANTHER; PTHR10629; PTHR10629; 1.
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   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    430       Modification methylase Sau96I.
FT                                /FTId=PRO_0000087908.
FT   DOMAIN        9     63       HTH cro/C1-type.
FT   DOMAIN       99    429       SAM-dependent MTase C5-type.
FT   ACT_SITE    174    174       By similarity.
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
//
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