T1M_SALPO
ID T1M_SALPO Reviewed; 529 AA.
AC P07989;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Type I restriction enzyme StySPI methylase subunit;
DE Short=M protein;
DE EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE AltName: Full=Type I methyltransferase M.StySPI {ECO:0000303|PubMed:12654995};
DE Short=M.StySPI {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type I restriction and modification system SP {ECO:0000303|PubMed:3025838};
GN Name=hsdM {ECO:0000303|PubMed:3025838}; Synonyms=hsdT;
OS Salmonella potsdam.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [GENOMIC DNA] OF 455-529, AND FUNCTION.
RX PubMed=3025838; DOI=10.1073/pnas.83.24.9368;
RA Fuller-Pace F.V., Murray N.E.;
RT "Two DNA recognition domains of the specificity polypeptides of a family of
RT type I restriction enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9368-9372(1986).
RN [3]
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 A-2 on the top strand and A-3
CC on the bottom strand of the sequence 5'-AACN(6)GTRC-3'. In the presence
CC of the R subunit the complex can also act as an endonuclease, binding
CC to the same target sequence but cutting the DNA some distance from this
CC site. Whether the DNA is cut or modified depends on the methylation
CC state of the target sequence. When the target site is unmodified, the
CC DNA is cut. When the target site is hemimethylated, the complex acts as
CC a maintenance MTase modifying the DNA so that both strands become
CC methylated (PubMed:3025838, PubMed:12654995). After locating a non-
CC methylated recognition site, the enzyme complex serves as a molecular
CC motor that translocates DNA in an ATP-dependent manner until a
CC collision occurs that triggers cleavage (By similarity).
CC {ECO:0000250|UniProtKB:P08957, ECO:0000269|PubMed:3025838,
CC 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; L02507; AAA27143.1; -; Genomic_DNA.
DR EMBL; M14984; AAA27144.1; -; Genomic_DNA.
DR AlphaFoldDB; P07989; -.
DR SMR; P07989; -.
DR REBASE; 3518; M.StySPI.
DR PRO; PR:P07989; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; -; 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 Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Restriction system; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..529
FT /note="Type I restriction enzyme StySPI methylase subunit"
FT /id="PRO_0000088025"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
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; 58906 MW; 07895A9ADA4FA249 CRC64;
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL PEGYRWDDLK
SRIGQEQLQF YRNLLVHLGA DEKKLVQAVF QNVNTTITQP KQLTELVSSM DSLDWYNGDH
GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF TPRPLIKTII HLLKPQPREV VQDPAAGTAG
FLIEADRYVK SQTNDLDDLD GDAQDFQIKK AFVGLELVPG TRRLALMNCL LHDIEGNLDH
GGAIRLGNTL GSDGENLPQA DIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL
PPGGRAAAVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV KTNVLFFTKG
TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP FETVYGEDPH GLSPRTEGEW
SFNAEESEVA DSEENKNADQ HQATSRWRKF SREWIRTAKS DSLDISWLKD KDSIDADSLP
EPDVLAAEAM GELVQALGEL DALMRELGAG DEADAQRQLL EEAFGGVKA
