MTM1_MYCGE
ID MTM1_MYCGE Reviewed; 317 AA.
AC Q49400; Q49252;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Type II methyltransferase M.MgeORF184P {ECO:0000303|PubMed:12654995};
DE Short=M.MgeORF184P {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.72 {ECO:0000305|PubMed:23300489};
DE AltName: Full=Type II methyltransferase M.MgeI {ECO:0000303|PubMed:23300489};
DE Short=M.MgeI {ECO:0000303|PubMed:23300489};
GN OrderedLocusNames=MG184;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-240.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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 PROBABLE FUNCTION, GENOME METHYLATION, AND DISCUSSION OF SEQUENCE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
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: Probably recognizes the double-stranded sequence 5'-CTAT-3'
CC and methylates A-3 on only one strand; as the bacterial DNA is
CC methylated on this sequence and this is the only type II methylase in
CC the genome, it is probably responsible for all of the methylation on
CC this site in the genome. {ECO:0000250|UniProtKB:Q50290,
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:0000250|UniProtKB:Q50290, ECO:0000305|PubMed:23300489};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L43967; AAC71403.1; -; Genomic_DNA.
DR EMBL; U02115; AAD12389.1; -; Genomic_DNA.
DR PIR; D64220; D64220.
DR RefSeq; WP_010869363.1; NC_000908.2.
DR AlphaFoldDB; Q49400; -.
DR STRING; 243273.MG_184; -.
DR REBASE; 257161; M.Ssp9304ORF3208P.
DR REBASE; 78740; M.MgeORF184P.
DR EnsemblBacteria; AAC71403; AAC71403; MG_184.
DR KEGG; mge:MG_184; -.
DR eggNOG; ENOG502Z7VI; Bacteria.
DR HOGENOM; CLU_057063_0_0_14; -.
DR OMA; PRHYELY; -.
DR OrthoDB; 841118at2; -.
DR BioCyc; MGEN243273:G1GJ2-208-MON; -.
DR Proteomes; UP000000807; 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..317
FT /note="Type II methyltransferase M.MgeORF184P"
FT /id="PRO_0000088015"
SQ SEQUENCE 317 AA; 37053 MW; 7CBF45151ACD0B57 CRC64;
MHHFNRAKKA KNNEFFTLID EIENEVINYQ KQFANKTIFC NCNDGKNSHF FQFFQTNFNQ
LQLKKLIGFS FNNLSQADKF TFDGNKVTKT KLKGNGDFSS DESIEVLKQA DIVVTNPPFS
LFQSFIDLLI QHNKQFLVLG LNAAVSYNHI FTYFKTNKLW FGYTVNKTMS FSVNSDYQLY
NPKTSNFFTK NGKCFQKIAG ISWFTNLGKP HYNPFLNTNC FYKNNEKNYP KFDWYDAIYV
NKIKNIPMDW NGLMGVPLTF LNCYNPKQFE LVDCLANPYA TLDTLKTNAF VKLNQGDVRN
VNGKRRYVRV IIKKQQI
