ID   MTB1_BACAM              Reviewed;         423 AA.
AC   P23941;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 3.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Type II methyltransferase M.BamHI {ECO:0000303|PubMed:12654995};
DE            Short=M.BamHI {ECO:0000303|PubMed:1901989};
DE            EC=2.1.1.113 {ECO:0000269|PubMed:1901989};
DE   AltName: Full=Modification methylase BamHI;
DE   AltName: Full=N(4)- cytosine-specific methyltransferase BamHI;
GN   Name=bamHIM {ECO:0000303|PubMed:1901989};
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   422-LEU-GLU-423.
RC   STRAIN=ATCC 49763 / H;
RX   PubMed=1901989; DOI=10.1093/nar/19.4.841;
RA   Brooks J.E., Nathan P.D., Landry D., Sznyter L.A., White-Rees P.,
RA   Ives C.L., Moran L.S., Slatko B.E., Benner J.S.;
RT   "Characterization of the cloned BamHI restriction modification system: its
RT   nucleotide sequence, properties of the methylase, and expression in
RT   heterologous hosts.";
RL   Nucleic Acids Res. 19:841-850(1991).
RN   [2]
RP   SEQUENCE REVISION TO 28; 53; 167; 207 AND 348.
RA   Benner J.S.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-423.
RC   STRAIN=ATCC 49763 / H;
RX   PubMed=2235511; DOI=10.1093/nar/18.20.6145;
RA   Vanek P.G., Connaughton J.F., Kaloss W.D., Chirikjian J.G.;
RT   "The complete sequence of the Bacillus amyloliquefaciens strain H, cellular
RT   BamHI methylase gene.";
RL   Nucleic Acids Res. 18:6145-6145(1990).
RN   [4]
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'-GGATCC-3', methylates C-5 on both strands, and protects the
CC       DNA from cleavage by the BamHI endonuclease.
CC       {ECO:0000269|PubMed:1901989, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000269|PubMed:1901989};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         The protein is very stable, after 18 months at -20 degrees Celsius it
CC         retains 90% of its activity. {ECO:0000269|PubMed:1901989};
CC   -!- MISCELLANEOUS: The protein sequnce was determined following expression
CC       in E.coli. {ECO:0000269|PubMed:1901989}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA38200.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X55285; CAA38998.2; -; Genomic_DNA.
DR   EMBL; X54303; CAA38200.1; ALT_INIT; Genomic_DNA.
DR   PIR; S26843; S26843.
DR   RefSeq; WP_013353548.1; NZ_VRTX01000001.1.
DR   AlphaFoldDB; P23941; -.
DR   SMR; P23941; -.
DR   STRING; 692420.BAMF_3132; -.
DR   REBASE; 203429; M.Bat1359ORF4014P.
DR   REBASE; 203436; M.Bam1267ORF3424P.
DR   REBASE; 3293; M.BamHI.
DR   OrthoDB; 9800801at2; -.
DR   BRENDA; 2.1.1.113; 630.
DR   PRO; PR:P23941; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..423
FT                   /note="Type II methyltransferase M.BamHI"
FT                   /id="PRO_0000087920"
FT   REGION          397..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         422..423
FT                   /note="Missing: Has decreased methylase activity."
FT                   /evidence="ECO:0000269|PubMed:1901989"
SQ   SEQUENCE   423 AA;  49136 MW;  8C2D9F58F33E6669 CRC64;
     MRFFSVFDIV KNKANQLGYT ETEMYAVLKN YNVNKKDLLA YKENGVIPTD KVLNGILSYL
     GMTKVELELK LGRIPAGLED VFLNNTKEIA KILENKNSVK LNEFNSIQEI KPYFYTDLGK
     LYNGDCLELF KQVPDENVDT IFADPPFNLD KEYDEGVTDK NSFSGYLDWY YKWIDECIRV
     LKPGGSLFIY NIPKWNTYLS EYLNRKLNFR NWITVDMKFG LPIQNRLYPA NYSLLYYVKG
     DKPKTFNVQR IPLQTCPHCG REIKDYGGYK NKMNPKGVTL SDVWSDIYPV RHSSSKNRKF
     NELSVKLLDR IITMSTNEGD VVLDPFGGSG TTFAVSEMLG RKWIGFELGN CEIIKERLKN
     KDKDKKLLGK VYEEKNKLFP NRVKELRKKN GLWIDDDFRQ DHEGNSKGDK KNENNDQISL
     SLE
//