ID   MTL22_LACLC             Reviewed;         269 AA.
AC   P50178;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Type II methyltransferase M2.LlaDCHI {ECO:0000303|PubMed:12654995};
DE            Short=M2.LlaDCHI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase LlaDCHIB;
DE   AltName: Full=M.LlaIIB {ECO:0000303|PubMed:7793939};
DE   AltName: Full=Modification methylase LlaDCHIB;
DE            Short=M.LlaDCHIB {ECO:0000303|PubMed:7793939};
GN   Name=llaDCHIB {ECO:0000303|PubMed:7793939};
GN   Synonyms=llaIIB {ECO:0000303|PubMed:7793939};
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OG   Plasmid pSRQ700.
OC   Bacteria; Firmicutes; 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   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: A beta 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:7793939, 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; AAB06312.1; -; Genomic_DNA.
DR   RefSeq; NP_116732.1; NC_002798.1.
DR   RefSeq; WP_010925606.1; NZ_VBTA01000012.1.
DR   AlphaFoldDB; P50178; -.
DR   SMR; P50178; -.
DR   REBASE; 249492; M2.WciM2ORF523P.
DR   REBASE; 3663; M2.LlaDCHI.
DR   PRO; PR:P50178; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 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..269
FT                   /note="Type II methyltransferase M2.LlaDCHI"
FT                   /id="PRO_0000087954"
SQ   SEQUENCE   269 AA;  30925 MW;  0AB61895696B46EA CRC64;
     MAINEYKYGG VLMTKPYYEK ENAILVHADS FKLLEKIKPE SMDMIFADPP YFLSNGGMSN
     SGGQIVSVDK GDWDKISSFE EKHDFNRRWI RLARLVLKPN GTIWVSGSLH NIYSVGMALE
     QEGFKILNNI TWQKTNPAPN LSCRYFTHST ETILWARKND KKSRHYYNYE LMKEFNDGKQ
     MKDVWTGSLT KKSEKWAGKH PTQKPEYILE RIILASTKEN DYILDPFVGS GTTGVVAKRL
     GRKFIGIDSE KEYLKIAKKR LNKGATYGL