ID   T1ME_ECOLX              Reviewed;         490 AA.
AC   Q47282;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Type I restriction enzyme EcoEI methylase subunit {ECO:0000305};
DE            Short=M protein;
DE            EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE   AltName: Full=Type I methyltransferase M.EcoEI {ECO:0000303|PubMed:12654995};
DE            Short=M.EcoEI {ECO:0000303|PubMed:12654995};
GN   Name=hsdM;
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A58;
RX   PubMed=8412658; DOI=10.1111/j.1365-2958.1993.tb01675.x;
RA   Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.;
RT   "Conservation of motifs within the unusually variable polypeptide sequences
RT   of type I restriction and modification enzymes.";
RL   Mol. Microbiol. 9:133-143(1993).
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: 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(7)ATGC-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; L18759; AAD15049.1; -; Genomic_DNA.
DR   PIR; I41293; I41293.
DR   RefSeq; WP_058649287.1; NZ_NMFU01000051.1.
DR   AlphaFoldDB; Q47282; -.
DR   SMR; Q47282; -.
DR   REBASE; 101119; M.Rga602ORF2367P.
DR   REBASE; 157593; M.Rso10709ORF3042P.
DR   REBASE; 201010; M.RspNXC14ORF3392P.
DR   REBASE; 205293; M.Bso1395ORF934P.
DR   REBASE; 211745; M.RphB5ORF556P.
DR   REBASE; 211757; M.RspL182ORF1057P.
DR   REBASE; 233080; M.Sen4024ORF3807P.
DR   REBASE; 256765; M.Ssp9304ORF612P.
DR   REBASE; 3386; M.EcoEI.
DR   REBASE; 618856; M.LspCC1I.
DR   PRO; PR:Q47282; -.
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; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..490
FT                   /note="Type I restriction enzyme EcoEI methylase subunit"
FT                   /id="PRO_0000088021"
FT   BINDING         163..168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         193..195
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ   SEQUENCE   490 AA;  55620 MW;  A8643DEB39981FFB CRC64;
     MSISSVIKSL QDIMRKDAGV DGDAQRLGQL SWLLFLKIFD TQEEELELEQ DDYQFPIPQR
     YLWRSWAANS EGITGDALLE FVNDDLFPTL KNLTAPIDKN PRGFVVKQAF SDAYNYMKNG
     TLLRQVINKL NEIDFSSSQE RHLFGDIYEQ ILRDLQSAGN AGEFYTPRAV TRFMVNRIDP
     KLGESIMDPA CGTGGFLACA FDHVKDNYVK TTEDHKTLQQ QIYGVEKKQL PHLLCTTNML
     LHGIEVPVQI RHDNTLNKPL SSWDEQVDVI VTNPPFGGTE EDGIEKNFPA EMQTRETADL
     FLQLIIEVLA DKGRAAVVLP DGTLFGEGVK TKIKKLLTEE CNLHTIVRLP NGVFNPYTGI
     KTNILFFTKG QPTKEVWFYE HPYPDGVKNY SKTKPMKFEE FQAEIDWWGN EADDFASREE
     NNQAWKVGID DIIARNFNLD IKNPYQGETI SHDPDELLAQ YQTQQAEIGE LRNQLRDILG
     AALAGNKGAN
//