T1M_SALTY
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 03-AUG-2022, entry version 126.
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; Proteobacteria; 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 REBASE; 3516; M.StyLTIII.
DR REBASE; 3517; M.StySJI.
DR PaxDb; P40813; -.
DR EnsemblBacteria; AAL23343; AAL23343; 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-MON; -.
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; -; 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 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
