ID   MTM1_MYCPN              Reviewed;         319 AA.
AC   Q50290;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Type II methyltransferase M.MpnI {ECO:0000303|PubMed:23300489};
DE            Short=M.MpnI {ECO:0000303|PubMed:23300489};
DE            EC=2.1.1.72 {ECO:0000269|PubMed:23300489};
GN   Name=mte1 {ECO:0000303|PubMed:23300489}; OrderedLocusNames=MPN_198;
GN   ORFNames=GT9_orf319V, MP633;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8604303; DOI=10.1093/nar/24.4.628;
RA   Hilbert H., Himmelreich R., Plagens H., Herrmann R.;
RT   "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma
RT   pneumoniae comprising the dnaA region, the atp operon and a cluster of
RT   ribosomal protein genes.";
RL   Nucleic Acids Res. 24:628-639(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
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   [3]
RP   NOMENCLATURE.
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP   DNA-BINDING.
RC   STRAIN=ATCC 29342 / M129;
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: A methylase that recognizes the double-stranded sequence 5'-
CC       CTAT-3' and methylates A-3 on one strand; probably responsible for all
CC       of the methylation on this site in the genome.
CC       {ECO:0000269|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:0000269|PubMed:23300489};
CC   -!- INDUCTION: Detected after 6 and 96 hours growth, there are fewer copies
CC       at 96 hours (at protein level). {ECO:0000269|PubMed:23300489}.
CC   -!- DISRUPTION PHENOTYPE: Essential it cannot be disrupted.
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; U34795; AAC43683.1; -; Genomic_DNA.
DR   EMBL; U00089; AAB96281.1; -; Genomic_DNA.
DR   PIR; S62810; S62810.
DR   RefSeq; NP_109886.1; NC_000912.1.
DR   RefSeq; WP_010874555.1; NC_000912.1.
DR   AlphaFoldDB; Q50290; -.
DR   REBASE; 182809; M.DspNSZ14ORF526P.
DR   REBASE; 6710; M.MpnI.
DR   EnsemblBacteria; AAB96281; AAB96281; MPN_198.
DR   KEGG; mpn:MPN_198; -.
DR   PATRIC; fig|272634.6.peg.216; -.
DR   HOGENOM; CLU_057063_2_0_14; -.
DR   OMA; PRHYELY; -.
DR   BioCyc; MPNE272634:G1GJ3-316-MON; -.
DR   Proteomes; UP000000808; Chromosome.
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   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR025247; EcoRI-like_methylase.
DR   Pfam; PF13651; EcoRI_methylase; 2.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..319
FT                   /note="Type II methyltransferase M.MpnI"
FT                   /id="PRO_0000088018"
SQ   SEQUENCE   319 AA;  36870 MW;  C665CA40A958A78B CRC64;
     MHYFNRAKKA KNNEFYTLFE DIAAEVACYP NAFKGKVVLC NCNDGYQSNF WQFFQSQFHA
     LGLKKLVAIA FNPLGNSYQL NFDGKEIKEL PLAGNGSFDS AEAIVLLKQS DIVVTNPPFS
     LFQDFVCLLA EHGKQFLVLG HNGAVGYNQI FKLFKEEQLW YGHTVNSSML FQVQSNFKLY
     DPKSVNFVKK DGQLFQKVPG ISWFTNLKKN QQPAWLKTKS RYQGNEHKYP KFDWYDAIFV
     SKVKEIPLDW FGYMGVPLTF LNCFNPKQFE LIDCLANPYA TLDTLKTNAY VRSHHGDVRN
     VKGKRRYVRV VIKQRQNVI