T1MD_MYCPN
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 03-AUG-2022, entry version 131.
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) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
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 [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;
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; NC_000912.1.
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; 290905; M.Msa27082ORF3559P.
DR REBASE; 6703; M.MpnII.
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 OMA; YEYLMGM; -.
DR BioCyc; MPNE272634:G1GJ3-541-MON; -.
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; -; 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 Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00497; hsdM; 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
