ID   MTP2_NEIGO              Reviewed;         341 AA.
AC   P08455;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Type II methyltransferase M.NgoPII {ECO:0000303|PubMed:12654995};
DE            Short=M.NgoPII {ECO:0000303|PubMed:2837733};
DE            EC=2.1.1.37 {ECO:0000255|PROSITE-ProRule:PRU01016};
DE   AltName: Full=Cytosine-specific methyltransferase NgoPII;
DE   AltName: Full=Modification methylase NgoPII;
GN   Name=ngoPIIM; Synonyms=dcmB {ECO:0000303|PubMed:8406039};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=P9;
RX   PubMed=2837733; DOI=10.1093/nar/16.10.4369;
RA   Sullivan K.M., Saunders J.R.;
RT   "Sequence analysis of the NgoPII methyltransferase gene from Neisseria
RT   gonorrhoeae P9: homologies with other enzymes recognizing the sequence 5'-
RT   GGCC-3'.";
RL   Nucleic Acids Res. 16:4369-4387(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=P9;
RX   PubMed=2501649; DOI=10.1007/bf00334379;
RA   Sullivan K.M., Saunders J.R.;
RT   "Nucleotide sequence and genetic organization of the NgoPII restriction-
RT   modification system of Neisseria gonorrhoeae.";
RL   Mol. Gen. Genet. 216:380-387(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33084 / F62 / M-1914;
RX   PubMed=8406039; DOI=10.1016/0378-1119(93)90509-2;
RA   Gunn J.S., Stein D.C.;
RT   "Natural variation of the NgoII restriction-modification system of
RT   Neisseria gonorrhoeae.";
RL   Gene 132:15-20(1993).
RN   [4]
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).
CC   -!- FUNCTION: A methylase that recognizes the double-stranded sequence 5'-
CC       GGCC-3', methylates C-3 on both strands, and protects the DNA from
CC       cleavage by the NgoPII endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:2501649, ECO:0000305|PubMed:2837733}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; X06965; CAA30038.1; -; Genomic_DNA.
DR   EMBL; X52661; CAA36888.1; -; Genomic_DNA.
DR   EMBL; L14564; AAA17019.1; -; Unassigned_DNA.
DR   PIR; S00920; CTNHP2.
DR   RefSeq; WP_003690024.1; NZ_VAHL01000002.1.
DR   RefSeq; WP_003690326.1; NZ_LDOB01000089.1.
DR   AlphaFoldDB; P08455; -.
DR   REBASE; 3135; NgoLIIP.
DR   REBASE; 3464; M.NgoPII.
DR   REBASE; 3609; M.NgoLII.
DR   GeneID; 66754346; -.
DR   PRO; PR:P08455; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..341
FT                   /note="Type II methyltransferase M.NgoPII"
FT                   /id="PRO_0000087900"
FT   DOMAIN          12..341
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   341 AA;  38444 MW;  066DB246FF816D52 CRC64;
     MQNSSPTTYN PMKIISLFSG CGGLDLGFEK AGFEIPAANE YDKTIWATFK ANHPKTHLIE
     GDIRKIKEED FPEEIDGIIG GPPCQSWSEA GALRGIDDAR GQLFFDYIRI LKSKQPKFFL
     AENVSGMLAN RHNGAVQNLL KMFDGCGYDV TLTMANAKDY GVAQERKRVF YIGFRKDLEI
     KFSFPKGSTV EDKDKITLKD VIWDLQDTAV PSAPQNKTNP DAVNNNEYFT GSFSPIFMSR
     NRVKAWDEQG FTVQASGRQC QLHPQAPKME KHGANDYRFA AGKETLYRRM TVREVARIQG
     FPDNFKFIYQ NVNDAYKMIG NAVPVNLAYE IAAAIKKTLE R