ID   T1MD_MYCPN              Reviewed;         543 AA.
AC   P75436;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Type I restriction enzyme MpnII methylase subunit {ECO:0000305};
DE            Short=M protein;
DE            EC=2.1.1.72 {ECO:0000305|PubMed:23300489};
DE   AltName: Full=Type I methyltransferase M.MpnII {ECO:0000303|PubMed:23300489};
DE            Short=M.MpnII {ECO:0000303|PubMed:23300489};
GN   OrderedLocusNames=MPN_342; ORFNames=H91_orf543, MP494;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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).
RN   [3]
RP   FUNCTION, GENOME METHYLATION, SUBUNIT, INDUCTION, AND DNA-BINDING.
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=23300489; DOI=10.1371/journal.pgen.1003191;
RA   Lluch-Senar M., Luong K., Llorens-Rico V., Delgado J., Fang G., Spittle K.,
RA   Clark T.A., Schadt E., Turner S.W., Korlach J., Serrano L.;
RT   "Comprehensive methylome characterization of Mycoplasma genitalium and
RT   Mycoplasma pneumoniae at single-base resolution.";
RL   PLoS Genet. 9:e1003191-e1003191(2013).
CC   -!- FUNCTION: The subtype gamma methyltransferase (M) subunit of a type I
CC       restriction enzyme. The M and S subunits together form a
CC       methyltransferase (MTase) that probably methylates A-2 on the top
CC       strand and A-3 on the bottom strand of the sequence 5'-GAN(7)TAY-3'. As
CC       the bacterial DNA is methylated on this sequence and this is the only
CC       type I methylase in the genome, it is probably responsible for all of
CC       the methylation on this site in the genome. The R subunit has multiple
CC       frameshifts and is probably not expressed in this bacteria.
CC       {ECO:0000305|PubMed:23300489}.
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:0000305|PubMed:23300489};
CC   -!- SUBUNIT: The methyltransferase is composed of M and S polypeptides.
CC       {ECO:0000305|PubMed:23300489}.
CC   -!- INDUCTION: Detected at low levels after 6 and 96 hours growth, there
CC       are fewer copies at 96 hours (at protein level).
CC       {ECO:0000269|PubMed:23300489}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAB96142.1; -; Genomic_DNA.
DR   PIR; S73820; S73820.
DR   RefSeq; NP_110030.1; NC_000912.1.
DR   RefSeq; WP_010874698.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75436; -.
DR   SMR; P75436; -.
DR   IntAct; P75436; 2.
DR   STRING; 272634.MPN_342; -.
DR   REBASE; 154996; M.VscVS12ORF1031P.
DR   REBASE; 203439; M.Lpl434ORF2272P.
DR   REBASE; 203796; M.Ppe892ORF47P.
DR   REBASE; 290905; M.Msa27082ORF3559P.
DR   REBASE; 6703; M.MpnII.
DR   REBASE; 767817; M.SspSPORF2374P.
DR   EnsemblBacteria; AAB96142; AAB96142; MPN_342.
DR   KEGG; mpn:MPN_342; -.
DR   PATRIC; fig|272634.6.peg.366; -.
DR   HOGENOM; CLU_013049_0_1_14; -.
DR   OrthoDB; 9814572at2; -.
DR   BioCyc; MPNE272634:G1GJ3-541-MONOMER; -.
DR   PRO; PR:P75436; -.
DR   Proteomes; UP000000808; Chromosome.
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; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..543
FT                   /note="Type I restriction enzyme MpnII methylase subunit"
FT                   /id="PRO_0000088028"
FT   BINDING         208..213
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         240..242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ   SEQUENCE   543 AA;  61975 MW;  618EE22B4FE03064 CRC64;
     MEKKRTEQRN GVEKKIWEIA DKLRGTIDGW DFKSYVLIGL FYRFLSENLC KYFNDSERRN
     NPDFSYENLT DDYEAIDALK DAAIASKGFF IKPSQLFQNV VKSIRENKNN EDLNTTLRDI
     FDDIEKSTEL GDGRSKESFK GLFKDFNVSE VKLGSTLTIR TEKLKELLTS IDTMELDEFE
     KNSIDAFGDA YEFLISMYAQ NAGKSGGEFF TPQDISELLA RIAIGKKDTV DDVYDMACGS
     GSLLLQVIKV LGKEKTSLVS YYGQEINHTT YNLCRMNMIL HNIDYANFNI INADTLTTKE
     WEKHYVNCSN ENGFEVVVSN PPYSISWAGD KKSNLVSDVR FKDAGTLAPN SKADLAFVLH
     ALYVLGQEGT AAIVCFPGIL YREGKEQTIR KYLVDQNFVD AVIQLPSNLF STTSIATSIL
     VLKKNRDKKD PIFFIDGSNE FVREKKNNRL SPKNIEKIVD CFNSKKEEAN FAKSVERDKI
     RESNYDLTVG KYVNSEAEKE ELDIKVLNHS IDEIVDKQKD LRTKIKDIIQ DIKVDFDNID
     INN
//