MTD22_STREE
ID MTD22_STREE Reviewed; 268 AA.
AC P09358;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Type II methyltransferase M2.DpnII {ECO:0000303|PubMed:12654995};
DE Short=M2.DpnII {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.72 {ECO:0000269|PubMed:2687877};
DE AltName: Full=Adenine-specific methyltransferase DpnA {ECO:0000303|PubMed:2687877};
DE AltName: Full=M.DpnII 2;
DE AltName: Full=Modification methylase DpnIIB;
GN Name=dpnA {ECO:0000303|PubMed:2824782};
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=697;
RX PubMed=3019562; DOI=10.1016/0092-8674(86)90698-7;
RA Lacks S.A., Mannarelli B.M., Springhorn S.S., Greenberg B.;
RT "Genetic basis of the complementary DpnI and DpnII restriction systems of
RT S. pneumoniae: an intercellular cassette mechanism.";
RL Cell 46:993-1000(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), SEQUENCE REVISION TO
RP N-TERMINUS, AND ALTERNATIVE INITIATION.
RX PubMed=10712690; DOI=10.1046/j.1365-2958.2000.01777.x;
RA Lacks S.A., Ayalew S., de la Campa A.G., Greenberg B.;
RT "Regulation of competence for genetic transformation in Streptococcus
RT pneumoniae: expression of dpnA, a late competence gene encoding a DNA
RT methyltransferase of the DpnII restriction system.";
RL Mol. Microbiol. 35:1089-1098(2000).
RN [3]
RP PROTEIN SEQUENCE OF 1-13 (ISOFORM 1), FUNCTION, AND SUBUNIT.
RX PubMed=2824782; DOI=10.1016/0022-2836(87)90024-6;
RA de la Campa A.G., Purushottam K., Springhorn S.S., Lacks S.A.;
RT "Proteins encoded by the DpnII restriction gene cassette. Two methylases
RT and an endonuclease.";
RL J. Mol. Biol. 196:457-469(1987).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2687877; DOI=10.1073/pnas.86.23.9223;
RA Cerritelli S., Springhorn S.S., Lacks S.A.;
RT "DpnA, a methylase for single-strand DNA in the Dpn II restriction system,
RT and its biological function.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9223-9227(1989).
RN [5]
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 that recognizes the single- or
CC double-stranded sequence 5'-GATC-3', methylates A-2 on one or both
CC strands (respectively), and protects the DNA from cleavage by the DpnII
CC endonuclease. Further methylates DNA that is already methylated at 5'-
CC GATC-3' sites. Essential for establishment of a previously unmethylated
CC plasmid transformed into the cell as single-stranded DNA, enhances
CC plasmid transfer to DpnII-containing strains of Streptococcus
CC pneumoniae. {ECO:0000269|PubMed:2687877, ECO:0000269|PubMed:2824782,
CC ECO:0000303|PubMed:12654995}.
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 Evidence={ECO:0000269|PubMed:2687877, ECO:0000305|PubMed:2824782};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:2824782}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P09358-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09358-2; Sequence=VSP_018869;
CC -!- MISCELLANEOUS: The DpnII restriction system has two different
CC methylases. {ECO:0000269|PubMed:2824782}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced in response to the induction of
CC competence for genetic transformation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M14339; AAA88581.2; -; Genomic_DNA.
DR PIR; A24372; A24372.
DR RefSeq; WP_000794288.1; NZ_FHVM01000007.1. [P09358-1]
DR AlphaFoldDB; P09358; -.
DR SMR; P09358; -.
DR REBASE; 3637; M2.DpnII.
DR PATRIC; fig|1313.6513.peg.2192; -.
DR PRO; PR:P09358; -.
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 1: Evidence at protein level;
KW Alternative initiation; Direct protein sequencing; DNA-binding;
KW Methyltransferase; Restriction system; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..268
FT /note="Type II methyltransferase M2.DpnII"
FT /id="PRO_0000030349"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018869"
SQ SEQUENCE 268 AA; 30922 MW; DD039104E3A915FC CRC64;
MKNNEYKYGG VLMTKPYYNK NKMILVHSDT FKFLSKMKPE SMDMIFADPP YFLSNGGISN
SGGQVVSVDK GDWDKISSFE EKHEFNRKWI RLAKEVLKPN GTVWISGSLH NIYSVGMALE
QEGFKILNNI TWQKTNPAPN LSCRYFTHST ETILWARKND KKARHYYNYD LMKELNDGKQ
MKDVWTGSLT KKVEKWAGKH PTQKPEYLLE RIILASTKEG DYILDPFVGS GTTGVVAKRL
GRRFIGIDAE KEYLKIARKR LEAENETN
