ID   MTS1_STRSA              Reviewed;         653 AA.
AC   P29347;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Modification methylase StsI;
DE            Short=M.StsI {ECO:0000303|PubMed:1387204};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase StsI;
DE   AltName: Full=Type II methyltransferase M.StsI {ECO:0000303|PubMed:12654995};
GN   Name=stsIM;
OS   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=54;
RX   PubMed=1387204; DOI=10.1093/nar/20.16.4167;
RA   Kita K., Suisha M., Kotani H., Yanase H., Kato N.;
RT   "Cloning and sequence analysis of the StsI restriction-modification gene:
RT   presence of homology to FokI restriction-modification enzymes.";
RL   Nucleic Acids Res. 20:4167-4172(1992).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPE.
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: An alpha subtype methylase that recognizes the double-
CC       stranded sequence 5'-GGATG-3' in one strand and 3'-CATCC-5' in the
CC       other, methylates A of both strands, and protects the DNA from cleavage
CC       by the StsI endonuclease. The 2 domains of the protein participate in
CC       modification of the two strands. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:1387204}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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; D11101; BAA01876.1; -; Genomic_DNA.
DR   PIR; S35493; S35493.
DR   AlphaFoldDB; P29347; -.
DR   SMR; P29347; -.
DR   REBASE; 3512; M.StsI.
DR   PRIDE; P29347; -.
DR   PRO; PR:P29347; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1020.10; -; 2.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR012186; Ade-mod_methylase_MStsI.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30481; PTHR30481; 2.
DR   Pfam; PF02086; MethyltransfD12; 2.
DR   PIRSF; PIRSF036638; M_m6A_StsI; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   TIGRFAMs; TIGR00571; dam; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Repeat; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..653
FT                   /note="Modification methylase StsI"
FT                   /id="PRO_0000087962"
SQ   SEQUENCE   653 AA;  76068 MW;  C4D42B76E5665E91 CRC64;
     MRYIGSKKLL LPEIKKMVDK HTDGSEEVFL DLFAGTNVVA NYFKQFYTVY SNDMLFFSYV
     NAKATIENNS KPSFSKLIQA GISSPMTYLQ NLEVNDETIG YYEVAYSPTG EANYLSVHNA
     KKLDIIRSQI ESWKNQNLLT EHEYYYLLSS LIEALPFISN TTGTYGAFLK HWDKRSLNDL
     ELQDFTIFDN SKQNKAFNED ANELVQKIKA DIVYIDTPYN SRQYASNYHL LENVARNEHP
     TLKGITKIFD WKNLKSDYAT KGKALVAMRD LIQNINSTHI ILSYNNEGII SEEDLTNILK
     EFSVDGIVDI KKIPYRKYQS KNVSKNKEIY ELLFYIQRKP FSKNKTLNKP LNNVRVSSTK
     KYIKSPLNYI GGKYKLLNQI LPLFPKNINT FVDIFSGGAN VGINVKAKKY IFNDMNTRIN
     EMFRYFQTQP PVKLVQQIEE KIDEWGLSKT NEDAFLAFRK HYNTNPNPLD LYVLSSFSYN
     YQFRFNNSME FNNPFGRNRS HFSENMRNNL LNFVTKLQTL DATFTDNYFN EFDFSNLTSN
     DFIYLDPPYL ITTGSYNDGK RGFSDWNNTS EMKLLNFMDY LNQHGIRFAL SNVTEHKGKT
     NQLLKDWAYS RNLNVNYLDH NYNNSSHNSK SKGSQEVLIT NYETKTFNLL NTK