ID   T1M_SALTY               Reviewed;         529 AA.
AC   P40813; Q6LAL9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Type I restriction enzyme StySJI methylase subunit;
DE            Short=M protein;
DE            EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE   AltName: Full=Type I methyltransferase M.StySJI {ECO:0000303|PubMed:12654995};
DE            Short=M.StySJI {ECO:0000303|PubMed:12654995};
DE   AltName: Full=Type I restriction and modification system SB {ECO:0000303|PubMed:2838725};
GN   Name=hsdM {ECO:0000303|PubMed:2838725}; Synonyms=hsdT;
GN   OrderedLocusNames=STM4525;
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=LT2;
RX   PubMed=1409708; DOI=10.1073/pnas.89.20.9836;
RA   Sharp P.M., Kelleher J.E., Daniel A.S., Cowan G.M., Murray N.E.;
RT   "Roles of selection and recombination in the evolution of type I
RT   restriction-modification systems in enterobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9836-9840(1992).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-529.
RC   STRAIN=LT2;
RX   PubMed=2838725; DOI=10.1111/j.1365-2958.1987.tb00521.x;
RA   Gann A.A.F., Campbell A.J.B., Collins J.F., Coulson A.F.W., Murray N.E.;
RT   "Reassortment of DNA recognition domains and the evolution of new
RT   specificities.";
RL   Mol. Microbiol. 1:13-22(1987).
RN   [4]
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: The subtype gamma methyltransferase (M) subunit of a type I
CC       restriction enzyme. The M and S subunits together form a
CC       methyltransferase (MTase) that methylates two adenine residues of the
CC       sequence 5'-GAGN(6)GTRC-3'. In the presence of the R subunit the
CC       complex can also act as an endonuclease, binding to the same target
CC       sequence but cutting the DNA some distance from this site. Whether the
CC       DNA is cut or modified depends on the methylation state of the target
CC       sequence. When the target site is unmodified, the DNA is cut. When the
CC       target site is hemimethylated, the complex acts as a maintenance MTase
CC       modifying the DNA so that both strands become methylated. After
CC       locating a non-methylated recognition site, the enzyme complex serves
CC       as a molecular motor that translocates DNA in an ATP-dependent manner
CC       until a collision occurs that triggers cleavage.
CC       {ECO:0000250|UniProtKB:P08957, 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:0000250|UniProtKB:P08957};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S; the restriction enzyme has stoichiometry
CC       R(2)M(2)S(1) while the methyltransferase is M(2)S(1).
CC       {ECO:0000250|UniProtKB:P08957}.
CC   -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC       multifunctional systems which require ATP, S-adenosyl methionine and
CC       Mg(2+) as cofactors and, in addition to their endonucleolytic and
CC       methylase activities, are potent DNA-dependent ATPases.
CC       {ECO:0000250|UniProtKB:P08957}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; L02506; AAA19429.1; -; Unassigned_DNA.
DR   EMBL; AE006468; AAL23343.1; -; Genomic_DNA.
DR   EMBL; Y00524; CAA68579.1; -; Genomic_DNA.
DR   RefSeq; NP_463384.1; NC_003197.2.
DR   RefSeq; WP_001063190.1; NC_003197.2.
DR   AlphaFoldDB; P40813; -.
DR   SMR; P40813; -.
DR   STRING; 99287.STM4525; -.
DR   PaxDb; 99287-STM4525; -.
DR   GeneID; 1256051; -.
DR   KEGG; stm:STM4525; -.
DR   PATRIC; fig|99287.12.peg.4768; -.
DR   HOGENOM; CLU_018284_2_0_6; -.
DR   PhylomeDB; P40813; -.
DR   BioCyc; SENT99287:STM4525-MONOMER; -.
DR   PRO; PR:P40813; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..529
FT                   /note="Type I restriction enzyme StySJI methylase subunit"
FT                   /id="PRO_0000088026"
FT   REGION          405..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         148..153
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         178..180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ   SEQUENCE   529 AA;  59311 MW;  D5EF542069B8A88A CRC64;
     MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL PEGYRWDDLK
     SRIGQDQMQF YRNLLVQLGS DEKKLVQAVF HNVSTTIEQP KQLTELVSYM DALDWYNGNH
     GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF TPRPLIKTII HLLKPQPREV VQDPAAGTAG
     FLIEADRYVK SQTNDLDDLD GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH
     GGAIRLGNTL GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL
     HPGGRAAVVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV KTNVLFFTKG
     TVTNPHQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP FETVYGEDPH GLSPREEGEW
     SFNAEESEVA DSEENKNTDQ HQATSRWRKF SREWIRSAKS DSLDISWLKD KDSIDADSLP
     EPDVLAAEAM GELVQALGEL DALMRELGAG DEADAQRQLL NEAFGEVKA
//