ID MTB2_BACAM Reviewed; 265 AA. AC P18051; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 22-FEB-2023, entry version 95. DE RecName: Full=Orphan methyltransferase M.BamHII {ECO:0000303|PubMed:12654995}; DE Short=M.BamHII {ECO:0000303|PubMed:12654995}; DE EC=2.1.1.113; DE AltName: Full=Modification methylase BamHII; DE AltName: Full=N(4)-cytosine-specific methyltransferase BamHII; GN Name=bamHIIM; OS Bacillus amyloliquefaciens (Bacillus velezensis). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus amyloliquefaciens group. OX NCBI_TaxID=1390; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=H; RX PubMed=2374727; DOI=10.1093/nar/18.13.4002; RA Connaughton J.F., Kaloss W.D., Vanek P.G., Nardone G.A., Chirikjian J.G.; RT "The complete sequence of the Bacillus amyloliquefaciens proviral H2, BamHI RT methylase gene."; RL Nucleic Acids Res. 18:4002-4002(1990). 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'-GGATCC-3', methylates C-? on both strands. No endonuclease CC has been identified for this methylase, although it is speculated it CC might protect against BamHI. {ECO:0000303|PubMed:12654995, CC ECO:0000305|PubMed:2374727}. 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 -!- MISCELLANEOUS: This methylase is encoded on the proviral phage H2. CC {ECO:0000269|PubMed:2374727}. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4) CC subfamily. {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; X53032; CAA37205.1; -; Genomic_DNA. DR PIR; S10316; S10316. DR AlphaFoldDB; P18051; -. DR SMR; P18051; -. DR REBASE; 157607; M2.Rso10709ORF7P. DR REBASE; 186; M.BamHII. DR REBASE; 204726; M.Bso1395ORF2761P. DR BRENDA; 2.1.1.113; 630. DR PRO; PR:P18051; -. 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methyltransferase. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00093; N4_MTASE; 1. PE 3: Inferred from homology; KW DNA-binding; Methyltransferase; Restriction system; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..265 FT /note="Orphan methyltransferase M.BamHII" FT /id="PRO_0000087921" SQ SEQUENCE 265 AA; 30981 MW; 895A51217A814820 CRC64; MKENIGDCTI DLTVTSPPYD DLRNYNGYSF NFEETAQELY RVTKEGGVVV WVVGDKTHKG SETGSSFRQA LYFKELGFNL HDTMIYEKDS ISFPDKNRYY QIFEYMFIFS KGKPKTINLL ADRKNKWYNG KKHIKGHYRK MDGEKVRHHK QNLLKEFGVR FNIWRIPNGH QKSTLDKIAF QHPAIFPEKL AEDHILSWSN EGDIVFDPFM GSGTTAKMAA LNNRKYIGTE ISKEYCDIAN ERLKNYIILH KRMEGKGYRL PQVHS //