ID   MTB1_BREEP              Reviewed;         403 AA.
AC   P10283;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   13-SEP-2023, entry version 96.
DE   RecName: Full=Type II methyltransferase M.BepI {ECO:0000303|PubMed:12654995};
DE            Short=M.BepI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:2784204};
DE   AltName: Full=Cytosine-specific methyltransferase BepI;
DE   AltName: Full=Modification methylase BepI;
GN   Name=bepIM;
OS   Brevibacterium epidermidis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=R/Szeged;
RX   PubMed=2784204; DOI=10.1093/nar/17.3.1077;
RA   Kupper D., Zhou J.-G., Venetianer P., Kiss A.;
RT   "Cloning and structure of the BepI modification methylase.";
RL   Nucleic Acids Res. 17:1077-1088(1989).
RN   [2]
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, recognizes the double-stranded sequence 5'-CGCG-
CC       3', methylates C-1 on both strands, and protects the DNA from cleavage
CC       by the BepI endonuclease. {ECO:0000269|PubMed:2784204,
CC       ECO:0000303|PubMed:12654995}.
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         ECO:0000269|PubMed:2784204};
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; X13555; CAA31907.1; -; Genomic_DNA.
DR   PIR; S02856; S02856.
DR   AlphaFoldDB; P10283; -.
DR   SMR; P10283; -.
DR   REBASE; 3301; M.BepI.
DR   PRO; PR:P10283; -.
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; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..403
FT                   /note="Type II methyltransferase M.BepI"
FT                   /id="PRO_0000087870"
FT   DOMAIN          1..400
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   403 AA;  45466 MW;  666CEE1C1C69922E CRC64;
     MKVLSLFSGC GGMDLGLEGG FLAHRSSINS DLYASYISDH DENYVYLKKT GFETVFANDI
     LPFAKLAWCN FFKNRVNQPE NIFHLESIVD VVNNIENKQF SFPNDIDVVT GGFPCQDFSF
     AGKRKGFDSH KDHNGIIYNE PTEATRGQLY LWLKKVVEIT KPKVFIAENV KGLVTLGDVK
     DIIQKDFRNI DDGYVVLDAQ VLNAKNYGVA QNRERVIFIG ISKRYANKKI LDELISLQEK
     SEVYPYPPYT HGTDPELKPY ATLNQILAHL PEPELASTDK SQQSYSKAKL FKKTQGNIEV
     NMNGQAPTIR AEHHGNIEFR RLSKENGGTN LSELHLPQRR LTVRECALIQ SFPPDYEFVF
     NYGKANSVSA SAAYKIIGNA VPPLLGFAIG RHLSQIWDKL FKT
//