MTL21_LACLC
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 03-AUG-2022, entry version 96.
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; 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 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; -; 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 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
