ID   MTK1_KLEPN              Reviewed;         417 AA.
AC   P25238;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Type II methyltransferase M.KpnI {ECO:0000303|PubMed:12654995};
DE            Short=M.KpnI {ECO:0000303|PubMed:1754388};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase KpnI;
DE   AltName: Full=Modification methylase KpnI;
GN   Name=kpnIM {ECO:0000303|PubMed:1754388};
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OK8;
RX   PubMed=1754388; DOI=10.1093/nar/19.23.6505;
RA   Chatterjee D.K., Hammond A.W., Blakesley R.W., Adams S.M., Gerard G.F.;
RT   "Genetic organization of the KpnI restriction-modification system.";
RL   Nucleic Acids Res. 19:6505-6509(1991).
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).
CC   -!- FUNCTION: A beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-GGTACC-3', methylates A-4 on both strands, and protects the
CC       DNA from cleavage by the KpnI endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M76435; AAA25090.1; -; Genomic_DNA.
DR   EMBL; X61796; CAA43898.1; -; Genomic_DNA.
DR   PIR; S34433; S34433.
DR   RefSeq; WP_004176757.1; NZ_ULCW01000003.1.
DR   AlphaFoldDB; P25238; -.
DR   SMR; P25238; -.
DR   REBASE; 231989; M.Sen4024ORF3837P.
DR   REBASE; 3436; M.KpnI.
DR   PRO; PR:P25238; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Restriction system; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..417
FT                   /note="Type II methyltransferase M.KpnI"
FT                   /id="PRO_0000087966"
SQ   SEQUENCE   417 AA;  47577 MW;  42BFAA6F772347BD CRC64;
     MDNHANEINK LSRELGLLSN YEFNMDELKN LSPLDSTSSS IYIGDNLTYL QGLSKTSPKT
     IDFCYIDPPY NTGNKIIYHD NRKSVSSDIF GLHNEWMSFL LPRLFHAHKM LKDTGIIAIS
     IDDYEFAHLK ILMDKIFGED NFIGNIVVCR SKNGKGSKRN IASAHEYLLV YGKSDMAELS
     GQPDDKSLYD KVDCFGEYRI DGMFRKKGDS SLRTDRPNMF YPLYFNPSTG EVQVEPELGL
     KTVYPIDSKG IERRWLWSKE TARERSWELF ASKNGVVYVK NYSSSHKRIK VRTLWNDSSF
     YTERATNEIT KIFGSKVFDT PKALNYIMSI INCMAKPDAL ILDFFAGSGT TAHAAAVLNS
     LDGGSRKTIL MESNHPITKT HIAYKSGFRK ISDITISRLN YVSDNFPDFK YKKIEII