ID   DMA_SALTM               Reviewed;         278 AA.
AC   P0DMP4; P0A291; P55893;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 22.
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=M.StyDam;
GN   Name=dam;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF 269-GLN--LYS-278.
RC   STRAIN=wt220;
RX   PubMed=9575240; DOI=10.1007/s002030050607;
RA   Brawer R., Batista F.D., Burrone O.R., Sordelli D.O., Cerquetti M.C.;
RT   "A temperature-sensitive DNA adenine methyltransferase mutant of Salmonella
RT   typhimurium.";
RL   Arch. Microbiol. 169:530-533(1998).
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       May be involved in methyl-directed DNA mismatch repair, initiation of
CC       chromosome replication and gene expression (By similarity).
CC       {ECO:0000250|UniProtKB:P0AEE8, ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:9575240}.
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: Cells are more sensitive to mutagenic agents.
CC       {ECO:0000269|PubMed:9575240}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U76993; AAB19116.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DMP4; -.
DR   SMR; P0DMP4; -.
DR   REBASE; 2891; M.StyADam.
DR   eggNOG; COG0338; Bacteria.
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   1: Evidence at protein level;
KW   DNA replication; DNA-binding; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..278
FT                   /note="DNA adenine methylase"
FT                   /id="PRO_0000430427"
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         269..278
FT                   /note="Missing: In D220; temperature-sensitive, grows at 28
FT                   but less well at 37 degrees Celsius, cells are
FT                   filamentous."
FT                   /evidence="ECO:0000269|PubMed:9575240"
SQ   SEQUENCE   278 AA;  31968 MW;  900F4B77D825E38A CRC64;
     MKKNRAFLKW AGGKYPLLDD IKRHLPKGEC LVEPFVGAGS VFLNTDFSRY ILADINSDLI
     SLYNIVKLRT DEYVQASREL FMPETNQAEV YYQLREEFNT CQDPFRRAVL FLYLNRYGYN
     GLCRYNLRGE FNVPFGRYKR PYFPEAELYH FAEKAQNAFF YCESYADSMA RADKSSVVYC
     DPPYAPLSAT ANFTAYHTNS FSLTQQAHLA EIAENLVSNR IPVLISNHDT ALTREWYQLA
     KLHVVKVRPS ISSNGGTRKK VDELLALYQP GVATPARK