ID   MTL21_LACLC             Reviewed;         284 AA.
AC   P50179; Q93K25;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   13-SEP-2023, entry version 100.
DE   RecName: Full=Type II methyltransferase M1.LlaDCHI {ECO:0000303|PubMed:12654995};
DE            Short=M1.LlaDCHI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase LlaDCHIA;
DE   AltName: Full=M.LlaIIA {ECO:0000303|PubMed:7793939};
DE   AltName: Full=Modification methylase LlaDCHIA;
DE            Short=M.LlaDCHIA {ECO:0000303|PubMed:11467810};
GN   Name=llaDCHIA {ECO:0000303|PubMed:11467810};
GN   Synonyms=llaDCHIAM, llaIIA {ECO:0000303|PubMed:7793939};
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OG   Plasmid pSRQ700.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DCH-4;
RX   PubMed=7793939; DOI=10.1128/aem.61.6.2193-2202.1995;
RA   Moineau S., Walker S.A., Vedamuthu E.R., Vandenbergh P.A.;
RT   "Cloning and sequencing of LlaDCHI restriction/modification genes from
RT   Lactococcus lactis and relatedness of this system to the Streptococcus
RT   pneumoniae DpnII system.";
RL   Appl. Environ. Microbiol. 61:2193-2202(1995).
RN   [2]
RP   ERRATUM OF PUBMED:7793939.
RA   Moineau S., Walker S.A., Vedamuthu E.R., Vandenbergh P.A.;
RL   Appl. Environ. Microbiol. 61:3514-3514(1995).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=11467810; DOI=10.3168/jds.s0022-0302(01)74595-x;
RA   Boucher I., Emond E., Parrot M., Moineau S.;
RT   "DNA sequence analysis of three Lactococcus lactis plasmids encoding phage
RT   resistance mechanisms.";
RL   J. Dairy Sci. 84:1610-1620(2001).
RN   [4]
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', methylates A-2 on both strands, and protects the
CC       DNA from cleavage by the LlaDCHI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:7793939}.
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   -!- MISCELLANEOUS: The LlaDCHI restriction system has two different
CC       methylases. {ECO:0000269|PubMed:7793939}.
CC   -!- MISCELLANEOUS: Genes encoded on plasmid pSQR700 confer strong
CC       resistance to the three most common lactococcal phage species (936, c2,
CC       and P335). Its presence is probably one reason for the strong
CC       bacteriophage resistance shown by strain DCH-4 over the years.
CC       {ECO:0000305|PubMed:7793939}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U16027; AAK57808.1; -; Genomic_DNA.
DR   RefSeq; NP_116733.1; NC_002798.1.
DR   RefSeq; WP_010925605.1; NZ_VBTA01000012.1.
DR   AlphaFoldDB; P50179; -.
DR   SMR; P50179; -.
DR   REBASE; 249493; M1.WciM2ORF523P.
DR   REBASE; 290974; M.Msa27082ORF4226P.
DR   REBASE; 3662; M1.LlaDCHI.
DR   PRO; PR:P50179; -.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..284
FT                   /note="Type II methyltransferase M1.LlaDCHI"
FT                   /id="PRO_0000087953"
FT   BINDING         17
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  33078 MW;  C46064217FC4FB09 CRC64;
     MNLLQKNKIN LRPFTKWTGG KRQLLPHIQY LMPEKYNHFF EPFIGGGALF FELAPQKAVI
     NDFNSELINC YRQMKDNPEQ LIELLTNHQR ENSKEYYLDL RSSDRDGRID KMSEVERAAR
     IMYMLRVDFN GLYRVNSKNQ FNVPYGRYKN PKIVDKELIE SISEYLNNNS IKIMSGDFEK
     AVKEAQDGDF VYFDPPYIPL SETSAFTSYT HEGFSYEDQV RLRDCFKQLD SKGVFVMLSN
     SSSPLAEELY KDFNIHKIEA TRTNGAKSSS RGKITEIIVT NYGN
//