DMA_ECO57
ID DMA_ECO57 Reviewed; 278 AA.
AC P0AEE9; P00475;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA adenine methylase;
DE EC=2.1.1.72;
DE AltName: Full=DNA adenine methyltransferase;
DE AltName: Full=Deoxyadenosyl-methyltransferase;
DE AltName: Full=Orphan methyltransferase M.EcoO157DamP/M.EcoKO157DamP {ECO:0000303|PubMed:12654995};
DE Short=M.EcoO157DamP/M.EcoKO157DamP {ECO:0000303|PubMed:12654995};
GN Name=dam; OrderedLocusNames=Z4740, ECs4229;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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: An alpha subtype methylase, recognizes the double-stranded
CC sequence 5'-GATC-3' and methylates A-2 (By similarity)
CC (PubMed:12654995). May be involved in methyl-directed DNA mismatch
CC repair, initiation of chromosome replication and gene expression (By
CC similarity). {ECO:0000250|UniProtKB:P0AEE8,
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG58487.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37652.1; -; Genomic_DNA.
DR PIR; C86003; C86003.
DR PIR; E91157; E91157.
DR RefSeq; NP_312256.1; NC_002695.1.
DR RefSeq; WP_000742143.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEE9; -.
DR SMR; P0AEE9; -.
DR STRING; 155864.EDL933_4585; -.
DR REBASE; 154998; M.VscVS12DamP.
DR REBASE; 155474; M.VscVS05DamP.
DR REBASE; 232309; M.Sen4024DamP.
DR REBASE; 232684; M.Sen4839ORF1762P.
DR REBASE; 232686; M.Sen4839DamP.
DR REBASE; 252454; M.Ssp8227ORF2746P.
DR REBASE; 5029; M.EcoO157DamP.
DR REBASE; 5592; M.EcoKO157DamP.
DR EnsemblBacteria; AAG58487; AAG58487; Z4740.
DR EnsemblBacteria; BAB37652; BAB37652; ECs_4229.
DR GeneID; 66672733; -.
DR GeneID; 915915; -.
DR KEGG; ece:Z4740; -.
DR KEGG; ecs:ECs_4229; -.
DR PATRIC; fig|386585.9.peg.4415; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_0_1_6; -.
DR OMA; MNRHGFN; -.
DR BRENDA; 2.1.1.72; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1020.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; PTHR30481; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00571; dam; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..278
FT /note="DNA adenine methylase"
FT /id="PRO_0000087992"
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 32100 MW; B2FA5D1FDC863CB9 CRC64;
MKKNRAFLKW AGGKYPLLDD IKRHLPKGEC LVEPFVGAGS VFLNTDFSRY ILADINSDLI
SLYNIVKMRT DEYVQAAREL FVPETNCAEV YYQFREEFNK SQDPFRRAVL FLYLNRYGYN
GLCRYNLRGE FNVPFGRYKK PYFPEAELYH FAEKAQNAFF YCESYADSMA RADDASVVYC
DPPYAPLSAT ANFTAYHTNS FTLEQQAHLA EIAEGLVERH IPVLISNHDT MLTREWYQRA
KLHVVKVRRS ISSNGGTRKK VDELLALYKP GVVSPAKK
