ID   DCM_ECO57               Reviewed;         472 AA.
AC   P0AEE0; P11876;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=DNA-cytosine methyltransferase;
DE            EC=2.1.1.37;
DE   AltName: Full=Probable type II methyltransferase M.Eco9331DcmP {ECO:0000303|PubMed:12654995};
DE            Short=M.Eco9331DcmP {ECO:0000303|PubMed:12654995};
GN   Name=dcm; OrderedLocusNames=Z3054, ECs2699;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
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.
CC       {ECO:0000250|UniProtKB:P0AED9}.
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   -!- 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; AE005174; AAG56975.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36122.1; -; Genomic_DNA.
DR   PIR; C85814; C85814.
DR   PIR; C90966; C90966.
DR   RefSeq; NP_310726.1; NC_002695.1.
DR   RefSeq; WP_001157239.1; NZ_VOAI01000028.1.
DR   AlphaFoldDB; P0AEE0; -.
DR   SMR; P0AEE0; -.
DR   STRING; 155864.Z3054; -.
DR   REBASE; 232038; M.Sen4024DcmP.
DR   REBASE; 232756; M.Sen4839DcmP.
DR   REBASE; 256726; M.Ssp9304ORF1801P.
DR   REBASE; 5031; M.EcoO157DcmP.
DR   REBASE; 5589; M.EcoKO157DcmP.
DR   GeneID; 75205799; -.
DR   GeneID; 913056; -.
DR   KEGG; ece:Z3054; -.
DR   KEGG; ecs:ECs_2699; -.
DR   PATRIC; fig|386585.9.peg.2828; -.
DR   eggNOG; COG0270; Bacteria.
DR   HOGENOM; CLU_006958_0_1_6; -.
DR   OMA; AGYRKGF; -.
DR   PRO; PR:P0AEE0; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 1.10.260.140; -; 1.
DR   Gene3D; 3.90.120.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF18284; DNA_meth_N; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
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_0000087914"
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
//