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 24-JAN-2024, entry version 137. 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}; GN OrderedLocusNames=b3387, JW3350; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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}. 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; 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; 511145-b3387; -. DR EnsemblBacteria; AAC76412; AAC76412; b3387. DR GeneID; 75206325; -. 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 OrthoDB; 9805629at2; -. DR PhylomeDB; P0AEE8; -. DR BioCyc; EcoCyc:EG10204-MONOMER; -. DR BioCyc; MetaCyc:EG10204-MONOMER; -. 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; Adenine-specific Methyltransferase, Domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00571; dam; 1. DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1. DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1. DR Pfam; PF02086; MethyltransfD12; 1. DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 FT S-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 //