ID   T3MO_SALTY              Reviewed;         652 AA.
AC   P40814;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Type III restriction-modification enzyme StyLTI Mod subunit;
DE            Short=M.StyLTI;
DE            EC=2.1.1.72 {ECO:0000269|PubMed:1995420};
DE   AltName: Full=StyLTI methyltransferase;
DE   AltName: Full=Type III methyltransferase M.StyLTI {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:1995420};
GN   Name=mod {ECO:0000303|PubMed:1846861}; OrderedLocusNames=STM0357;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT7;
RX   PubMed=8387444; DOI=10.1016/0378-1119(93)90623-b;
RA   Dartois V., de Backer O., Colson C.;
RT   "Sequence of the Salmonella typhimurium StyLT1 restriction-modification
RT   genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence
RT   of helicase domains.";
RL   Gene 127:105-110(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=LT7;
RX   PubMed=1995420; DOI=10.1016/0378-1119(91)90015-4;
RA   De Backer O., Colson C.;
RT   "Identification of the recognition sequence for the M.StyLTI
RT   methyltransferase of Salmonella typhimurium LT7: an asymmetric site typical
RT   of type-III enzymes.";
RL   Gene 97:103-107(1991).
RN   [4]
RP   FUNCTION.
RC   STRAIN=LT7;
RX   PubMed=1846861; DOI=10.1128/jb.173.3.1321-1327.1991;
RA   De Backer O., Colson C.;
RT   "Two-step cloning and expression in Escherichia coli of the DNA
RT   restriction-modification system StyLTI of Salmonella typhimurium.";
RL   J. Bacteriol. 173:1321-1327(1991).
RN   [5]
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: A beta subtype methylase that binds the system-specific DNA
CC       recognition site 5'-CAGAG-3' and methylates A-4 (of only 1 strand as
CC       the other does not have an A residue). DNA restriction requires both
CC       the Res and Mod subunits. {ECO:0000269|PubMed:1846861,
CC       ECO:0000269|PubMed:1995420, ECO:0000303|PubMed:12654995}.
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         Evidence={ECO:0000269|PubMed:1995420};
CC   -!- SUBUNIT: Homodimer, also forms a functional restriction-competent
CC       complex with Res. {ECO:0000250|UniProtKB:P12364}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M90544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE006468; AAL19311.1; -; Genomic_DNA.
DR   PIR; JN0657; JN0657.
DR   RefSeq; NP_459352.1; NC_003197.2.
DR   RefSeq; WP_000910371.1; NC_003197.2.
DR   AlphaFoldDB; P40814; -.
DR   SMR; P40814; -.
DR   STRING; 99287.STM0357; -.
DR   REBASE; 165434; M.Fba101ORF2038P.
DR   REBASE; 203812; M.Keu1446ORF2697P.
DR   REBASE; 231846; M.Sen4024ORF3354P.
DR   REBASE; 233833; M.Sen4839ORF3406P.
DR   REBASE; 3515; M.StyLTI.
DR   PaxDb; 99287-STM0357; -.
DR   GeneID; 1251876; -.
DR   KEGG; stm:STM0357; -.
DR   PATRIC; fig|99287.12.peg.378; -.
DR   HOGENOM; CLU_020164_2_0_6; -.
DR   OMA; KTHNAKP; -.
DR   PhylomeDB; P40814; -.
DR   BioCyc; SENT99287:STM0357-MONOMER; -.
DR   PRO; PR:P40814; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041405; T3RM_EcoP15I_C.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF16; TYPE III RESTRICTION-MODIFICATION ENZYME STYLTI MOD SUBUNIT; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   Pfam; PF18273; T3RM_EcoP15I_C; 1.
DR   PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..652
FT                   /note="Type III restriction-modification enzyme StyLTI Mod
FT                   subunit"
FT                   /id="PRO_0000088032"
FT   REGION          135..138
FT                   /note="Binding of S-adenosyl methionine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         55
FT                   /note="Missing (in strain: LT7)"
FT                   /evidence="ECO:0000269|PubMed:8387444"
FT   VARIANT         126
FT                   /note="A -> S (in strain: LT7)"
FT                   /evidence="ECO:0000269|PubMed:8387444"
SQ   SEQUENCE   652 AA;  73336 MW;  385DE4851545C84E CRC64;
     MLKDNQKHNE SVAPNSAFLS ELQRALPEFF TADRYNEQGE LIAKGGFDLA RFERALKARN
     IDELTSGYQI DFIGKDYAKK QAGEKSVTVI VPDVEHNTLA ENKNSHNLFL TGDNLDVLRH
     LQNNYADTVD MIYIDPPYNT GSDGFVYPDH FEYSDRALQD MFGLNDTELA RLKSIQGKST
     HSAWLSFMYP RLFLARKLLK DTGFIFISID DNEYANLKLM MDEIFGEGGF VTNVMWKRKK
     EISNDSDNVS IQGEYILVYA KTGQGALRLE PLSKEYIQKS YKEPTEQFPE GKWRPVPLTV
     SKGLSGGGYT YKITTPNGTV HERLWAYPEA SYQKLVADNL VYFGKDNGGI PQRVMYAHHS
     KGQPTTNYWD NVASNKEGKK EILDLFGDNV FDTPKPTALL KKIIKLAIDK DGVVLDFFAG
     SGTTAHAVMA LNEEDGGQRT FILCTIDQAL SNNTIAKKAG YNTIDEISRE RITRVAAKIR
     ANNPATNSDL GFKHYRFATP TQQTLDDLDS FDIATGHFIN TSGQLAAFTE SGFTDMINPF
     SARGLGVPGG ASGEETLLTT WLVADGYKMD IDVQTVDFSG YCARYVDNTR LYLIDERWGT
     EQTRDLLNHI GTHQLPVQTI VIYGYSFDLE SIRELEIGLK QLDQKVNLVK RY
//