MTB1_BREEP
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 03-AUG-2022, entry version 91.
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; Actinobacteria; Micrococcales; Brevibacteriaceae; 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; 3.40.50.150; -; 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 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
