DCM_ECOLI
ID DCM_ECOLI Reviewed; 472 AA.
AC P0AED9; P11876;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA-cytosine methyltransferase;
DE EC=2.1.1.37;
DE AltName: Full=Type II methyltransferase M.EcoKDcm {ECO:0000303|PubMed:12654995};
DE Short=M.EcoKDcm {ECO:0000303|PubMed:12654995};
GN Name=dcm {ECO:0000303|PubMed:2527357}; Synonyms=mec;
GN OrderedLocusNames=b1961, JW1944;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2527357; DOI=10.1093/nar/17.14.5844;
RA Hanck T., Gerwin N., Fritz H.-J.;
RT "Nucleotide sequence of the dcm locus of Escherichia coli K12.";
RL Nucleic Acids Res. 17:5844-5844(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2198248; DOI=10.1128/jb.172.8.4214-4221.1990;
RA Sohail A., Lieb M., Dar M., Bhagwat A.S.;
RT "A gene required for very short patch repair in Escherichia coli is
RT adjacent to the DNA cytosine methylase gene.";
RL J. Bacteriol. 172:4214-4221(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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 [5]
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 [6]
RP NOMENCLATURE.
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: This methylase recognizes the double-stranded sequence 5'-
CC CCWGG-3', methylates C-2 on both strands. {ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:2198248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- INTERACTION:
CC P0AED9; P06959: aceF; NbExp=3; IntAct=EBI-548525, EBI-542707;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; X13330; CAA31705.1; -; Genomic_DNA.
DR EMBL; M32307; AAA03723.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC75027.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15788.1; -; Genomic_DNA.
DR PIR; A37754; JS0263.
DR RefSeq; NP_416470.1; NC_000913.3.
DR RefSeq; WP_001157239.1; NZ_LN832404.1.
DR AlphaFoldDB; P0AED9; -.
DR SMR; P0AED9; -.
DR BioGRID; 4260865; 162.
DR BioGRID; 850830; 1.
DR DIP; DIP-47858N; -.
DR IntAct; P0AED9; 21.
DR STRING; 511145.b1961; -.
DR REBASE; 13374; M.EcoW3110DcmP.
DR REBASE; 175268; M.Rga4872ORF487P.
DR REBASE; 175271; M.Rga4872ORF19P.
DR REBASE; 2397; M.EcoKDcm.
DR jPOST; P0AED9; -.
DR PaxDb; P0AED9; -.
DR PRIDE; P0AED9; -.
DR EnsemblBacteria; AAC75027; AAC75027; b1961.
DR EnsemblBacteria; BAA15788; BAA15788; BAA15788.
DR GeneID; 946479; -.
DR KEGG; ecj:JW1944; -.
DR KEGG; eco:b1961; -.
DR PATRIC; fig|1411691.4.peg.291; -.
DR EchoBASE; EB0207; -.
DR eggNOG; COG0270; Bacteria.
DR HOGENOM; CLU_006958_0_1_6; -.
DR InParanoid; P0AED9; -.
DR OMA; AGYRKGF; -.
DR PhylomeDB; P0AED9; -.
DR BioCyc; EcoCyc:EG10211-MON; -.
DR BioCyc; MetaCyc:EG10211-MON; -.
DR BRENDA; 2.1.1.37; 2026.
DR PRO; PR:P0AED9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0090116; P:C-5 methylation of cytosine; IMP:EcoCyc.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR040743; DNA_meth_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF18284; DNA_meth_N; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..472
FT /note="DNA-cytosine methyltransferase"
FT /id="PRO_0000087913"
FT DOMAIN 87..457
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 472 AA; 53465 MW; 3635BFC001CF94B4 CRC64;
MQENISVTDS YSTGNAAQAM LEKLLQIYDV KTLVAQLNGV GENHWSAAIL KRALANDSAW
HRLSEKEFAH LQTLLPKPPA HHPHYAFRFI DLFAGIGGIR RGFESIGGQC VFTSEWNKHA
VRTYKANHYC DPATHHFNED IRDITLSHKE GVSDEAAAEH IRQHIPEHDV LLAGFPCQPF
SLAGVSKKNS LGRAHGFACD TQGTLFFDVV RIIDARRPAM FVLENVKNLK SHDQGKTFRI
IMQTLDELGY DVADAEDNGP DDPKIIDGKH FLPQHRERIV LVGFRRDLNL KADFTLRDIS
ECFPAQRVTL AQLLDPMVEA KYILTPVLWK YLYRYAKKHQ ARGNGFGYGM VYPNNPQSVT
RTLSARYYKD GAEILIDRGW DMATGEKDFD DPLNQQHRPR RLTPRECARL MGFEAPGEAK
FRIPVSDTQA YRQFGNSVVV PVFAAVAKLL EPKIKQAVAL RQQEAQHGRR SR
