DMA_ECOLI
ID DMA_ECOLI Reviewed; 278 AA.
AC P0AEE8; P00475; Q2M752;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA adenine methylase {ECO:0000303|PubMed:6300769};
DE EC=2.1.1.72;
DE AltName: Full=DNA adenine methyltransferase;
DE AltName: Full=Deoxyadenosyl-methyltransferase;
DE AltName: Full=Orphan methyltransferase M.EcoKDam {ECO:0000303|PubMed:12654995};
DE Short=M.EcoKDam {ECO:0000303|PubMed:12654995};
GN Name=dam {ECO:0000303|PubMed:6300769}; OrderedLocusNames=b3387, JW3350;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / CS520;
RX PubMed=6300769; DOI=10.1093/nar/11.3.837;
RA Brooks J.E., Blumenthal R.M., Gingeras T.R.;
RT "The isolation and characterization of the Escherichia coli DNA adenine
RT methylase (dam) gene.";
RL Nucleic Acids Res. 11:837-851(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7603433; DOI=10.1007/bf00290345;
RA Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT "Characterization of three genes in the dam-containing operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 247:546-554(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC STRAIN=K12;
RX PubMed=2549371; DOI=10.1007/bf00330946;
RA Jonczyk P., Hines R., Smith D.W.;
RT "The Escherichia coli dam gene is expressed as a distal gene of a new
RT operon.";
RL Mol. Gen. Genet. 217:85-96(1989).
RN [6]
RP MUTAGENESIS, MUTAGENESIS OF PRO-134; GLY-136; ARG-137; LYS-139; ASP-181;
RP PRO-182 AND PRO-183, AND DNA-BINDING.
RX PubMed=8341592; DOI=10.1093/nar/21.14.3183;
RA Guyot J.-B., Grassi J., Hahn U., Guschlbauer W.;
RT "The role of the preserved sequences of Dam methylase.";
RL Nucleic Acids Res. 21:3183-3190(1993).
RN [7]
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 that recognizes the double-
CC stranded sequence 5'-GATC-3' and methylates A-2 on both strands
CC (Probable) (PubMed:12654995). Although it shares sequence specificity
CC with a number of type II restriction endonucleases and methylases, it
CC is thought to act in methyl-directed mismatch repair, initiation of
CC chromosome replication and gene expression.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:6300769}.
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 -!- INTERACTION:
CC P0AEE8; P13035: glpD; NbExp=3; IntAct=EBI-548491, EBI-548509;
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; J01600; AAA23664.1; -; Genomic_DNA.
DR EMBL; V00272; CAA23530.1; -; Genomic_DNA.
DR EMBL; Z19601; CAA79668.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58184.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76412.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77904.1; -; Genomic_DNA.
DR EMBL; X15162; CAA33254.1; -; Genomic_DNA.
DR PIR; A00555; XYECDA.
DR RefSeq; NP_417846.1; NC_000913.3.
DR RefSeq; WP_000742143.1; NZ_STEB01000004.1.
DR PDB; 2G1P; X-ray; 1.89 A; A/B=1-278.
DR PDB; 2ORE; X-ray; 2.99 A; D/E/F=1-278.
DR PDB; 4GBE; X-ray; 2.66 A; D/E/F=1-278.
DR PDB; 4GOL; X-ray; 2.57 A; D/E/F=1-278.
DR PDB; 4GOM; X-ray; 2.45 A; D/E/F=1-278.
DR PDB; 4GON; X-ray; 2.72 A; D/E/F=1-278.
DR PDB; 4GOO; X-ray; 2.70 A; D/E/F=1-278.
DR PDB; 4RTJ; X-ray; 1.99 A; A=1-278.
DR PDB; 4RTK; X-ray; 1.96 A; A=1-278.
DR PDB; 4RTL; X-ray; 2.19 A; A=1-278.
DR PDB; 4RTM; X-ray; 2.50 A; A=1-278.
DR PDB; 4RTN; X-ray; 2.59 A; A=1-278.
DR PDB; 4RTO; X-ray; 2.69 A; A=1-278.
DR PDB; 4RTP; X-ray; 2.39 A; A=1-278.
DR PDB; 4RTQ; X-ray; 2.00 A; A=1-278.
DR PDB; 4RTR; X-ray; 2.39 A; A=1-278.
DR PDB; 4RTS; X-ray; 2.49 A; A=1-278.
DR PDBsum; 2G1P; -.
DR PDBsum; 2ORE; -.
DR PDBsum; 4GBE; -.
DR PDBsum; 4GOL; -.
DR PDBsum; 4GOM; -.
DR PDBsum; 4GON; -.
DR PDBsum; 4GOO; -.
DR PDBsum; 4RTJ; -.
DR PDBsum; 4RTK; -.
DR PDBsum; 4RTL; -.
DR PDBsum; 4RTM; -.
DR PDBsum; 4RTN; -.
DR PDBsum; 4RTO; -.
DR PDBsum; 4RTP; -.
DR PDBsum; 4RTQ; -.
DR PDBsum; 4RTR; -.
DR PDBsum; 4RTS; -.
DR AlphaFoldDB; P0AEE8; -.
DR SMR; P0AEE8; -.
DR BioGRID; 4261860; 125.
DR DIP; DIP-47948N; -.
DR IntAct; P0AEE8; 24.
DR STRING; 511145.b3387; -.
DR ChEMBL; CHEMBL1075075; -.
DR REBASE; 13376; M.EcoW3110DamP.
DR REBASE; 2396; M.EcoKDam.
DR REBASE; 441639; M.EcoBL21FDamP.
DR jPOST; P0AEE8; -.
DR PaxDb; P0AEE8; -.
DR PRIDE; P0AEE8; -.
DR EnsemblBacteria; AAC76412; AAC76412; b3387.
DR EnsemblBacteria; BAE77904; BAE77904; BAE77904.
DR GeneID; 66672733; -.
DR GeneID; 947893; -.
DR KEGG; ecj:JW3350; -.
DR KEGG; eco:b3387; -.
DR PATRIC; fig|1411691.4.peg.3343; -.
DR EchoBASE; EB0200; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_0_1_6; -.
DR InParanoid; P0AEE8; -.
DR OMA; MNRHGFN; -.
DR PhylomeDB; P0AEE8; -.
DR BioCyc; EcoCyc:EG10204-MON; -.
DR BioCyc; MetaCyc:EG10204-MON; -.
DR BRENDA; 2.1.1.72; 2026.
DR EvolutionaryTrace; P0AEE8; -.
DR PRO; PR:P0AEE8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IDA:EcoCyc.
DR GO; GO:1902328; P:bacterial-type DNA replication initiation; IMP:EcoCyc.
DR GO; GO:0032775; P:DNA methylation on adenine; IMP:EcoCyc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:EcoliWiki.
DR GO; GO:0006298; P:mismatch repair; IDA:EcoliWiki.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..278
FT /note="DNA adenine methylase"
FT /id="PRO_0000087991"
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"
FT MUTAGEN 134
FT /note="P->S: About 63% methylase activity, binds S-
FT adenosyl-methionine (SAM) normally."
FT /evidence="ECO:0000269|PubMed:8341592"
FT MUTAGEN 136
FT /note="G->A: About 33% methylase activity, binds SAM
FT normally."
FT /evidence="ECO:0000269|PubMed:8341592"
FT MUTAGEN 137
FT /note="R->L: No methylase activity, binds SAM normally."
FT /evidence="ECO:0000269|PubMed:8341592"
FT MUTAGEN 139
FT /note="K->S,T: 75% methylase activity, binds SAM normally."
FT /evidence="ECO:0000269|PubMed:8341592"
FT MUTAGEN 181
FT /note="D->G,N,S: Protein stable, no methylase activity, no
FT binding to S-adenosyl-methionine."
FT /evidence="ECO:0000269|PubMed:8341592"
FT MUTAGEN 183
FT /note="P->E,G: Low amounts of protein, no methyase
FT activity, no binding to S-adenosyl-methionine."
FT /evidence="ECO:0000269|PubMed:8341592"
FT MUTAGEN 183
FT /note="P->R: Protein stable, no methylase activity, no
FT binding to S-adenosyl-methionine."
FT /evidence="ECO:0000269|PubMed:8341592"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4GOM"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4GOM"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 203..218
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2G1P"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:2G1P"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:2G1P"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:2G1P"
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
