ID   DMA_SERMA               Reviewed;         270 AA.
AC   P45454;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
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.SmaII {ECO:0000303|PubMed:12654995};
DE            Short=M.SmaII {ECO:0000303|PubMed:12654995};
GN   Name=dam {ECO:0000303|PubMed:10383952};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Sr41;
RX   PubMed=10383952; DOI=10.1128/jb.181.13.3880-3885.1999;
RA   Ostendorf T., Cherepanov P., de Vries J., Wackernagel W.;
RT   "Characterization of a dam mutant of Serratia marcescens and nucleotide
RT   sequence of the dam region.";
RL   J. Bacteriol. 181:3880-3885(1999).
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: An alpha subtype methylase, recognizes the double-stranded
CC       sequence 5'-GATC-3' and methylates A-2 (Probable) (PubMed:12654995).
CC       Overexpression leads to hypermutability (PubMed:10383952). May be
CC       involved in methyl-directed DNA mismatch repair, initiation of
CC       chromosome replication and gene expression (Probable).
CC       {ECO:0000269|PubMed:10383952, ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:10383952}.
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   -!- DISRUPTION PHENOTYPE: Loss of N6-adenine methylation of 5'-GATC-3'
CC       sequences, more sensitive to multiple mutagenic agents.
CC       {ECO:0000269|PubMed:10383952}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X78412; CAA55177.1; -; Genomic_DNA.
DR   PIR; S47099; S47099.
DR   RefSeq; WP_033651736.1; NZ_VTUT01000009.1.
DR   AlphaFoldDB; P45454; -.
DR   SMR; P45454; -.
DR   STRING; 273526.SMDB11_3848; -.
DR   REBASE; 3001; M.SmaII.
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; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..270
FT                   /note="DNA adenine methylase"
FT                   /id="PRO_0000087997"
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   270 AA;  31331 MW;  8EEFFB163DF4288A CRC64;
     MKKNRAFLKW AGGKYPLVDE IRRHLPAGDC LIEPFVGAGS VFLNTDYDAY ILADINSDLI
     NLYNIVKLRT DDFVRDARTL FADEFNNSDQ FYLLREEFNT STEPYRRALL FLYLNRHCYN
     GLCRYNLRGE FNVPFGRYKK PYFPEEELYW FAEKSRNATF VCEHYRDTMA KAAAGAVVYC
     DPPYAPLSAT ANFTAYHTNS FSIADQQSLA HLAHQLSVES RVPVLISNHD TELTRDWYQH
     AALYVVKARR TISRNILGRS KVNELLALYR