ID   MTL1_LACLL              Reviewed;         622 AA.
AC   P35516;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-SEP-2023, entry version 93.
DE   RecName: Full=Modification methylase LlaI;
DE            Short=M.LlaI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase LlaI;
DE   AltName: Full=Type II methyltransferase M.LlaI {ECO:0000303|PubMed:12654995};
GN   Name=llaIM {ECO:0000303|PubMed:1906061};
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pTR2030.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ME2;
RX   PubMed=1906061; DOI=10.1128/jb.173.14.4363-4370.1991;
RA   Hill C., Miller L.A., Klaenhammer T.R.;
RT   "In vivo genetic exchange of a functional domain from a type II A methylase
RT   between lactococcal plasmid pTR2030 and a virulent bacteriophage.";
RL   J. Bacteriol. 173:4363-4370(1991).
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: An alpha subtype methylase that modifies unknown specific
CC       adenine residues, and protects the DNA from cleavage by the LlaI
CC       endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:1906061}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U17233; AAA65073.1; -; Genomic_DNA.
DR   PIR; S35122; S35122.
DR   AlphaFoldDB; P35516; -.
DR   SMR; P35516; -.
DR   REBASE; 3437; M.LlaI.
DR   PRO; PR:P35516; -.
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; 2.
DR   InterPro; IPR012186; Ade-mod_methylase_MStsI.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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; 2.
DR   PIRSF; PIRSF036638; M_m6A_StsI; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Plasmid; Repeat; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..622
FT                   /note="Modification methylase LlaI"
FT                   /id="PRO_0000087961"
SQ   SEQUENCE   622 AA;  72513 MW;  69A817F46BE9C772 CRC64;
     MRYLGNKTNL LNFIQQVIKK HDIQGQTFAD LFAGTGSVGD YFKGEYTVLS NDYMYFSKVI
     SEAKLLNSEK PKFDSFVKRY GKTPFQWLNE REYTPNDGYF VYNNYTPRAE RMYLTEENAL
     KIDGMRLDIE ELFQEGVISK AEYSYLLASL LESVTKVSNT SGTYQAFFKF WESRALKKFT
     IMPLEMKDSL SVSKDNRCFN KNTNRLVREI SGDIAYIDPP YTITQYTNSY HVLETIARYD
     NPELFGKTGR RVKREFSGYS NKSKAYYEFE DLFRQINFTH VLVSYSNQSI VPLDELVDLA
     RRFAVDGIVE VETNEYREYS TNNSSMKGEG KKLQEVIIYF KKNLETNKSP LNYAGSKDDV
     IPRIFKLLPK HVTTFVDAMG GAFNVGANRT ALNKVVYNEY HPFVFEMMQM IVNTPADELI
     RNVEQIVTRY SLEKKGKEAF NRLRDHYNNE EQTPINLYTL NIYSFQNILR FNQAKKYNTP
     IGNNEFNEGY KDRITRFVTR APEVEMRLGS YSAINFNEYD DDTVFYFDPP YLVTTAGYND
     GKRGFDGWDA EQEASLLKYL TELDSAGKKF MLSNVLEHKG KTNHLLMEWI QHHGFNVNTI
     GETGIKYPRR EILVTNYNTF ER
//