T4BA_WEICA
ID T4BA_WEICA Reviewed; 637 AA.
AC Q07605;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Type II restriction enzyme and methyltransferase RM.BcgI {ECO:0000303|PubMed:12654995};
DE EC=3.1.21.4 {ECO:0000269|PubMed:8451198};
DE AltName: Full=Restriction enzyme BgcI subunit A {ECO:0000303|PubMed:8276869};
DE Includes:
DE RecName: Full=Adenine-specific methyltransferase activity;
DE EC=2.1.1.72 {ECO:0000269|PubMed:8276869};
GN Name=bcgIA {ECO:0000303|PubMed:8276869};
OS Weizmannia coagulans (Bacillus coagulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Weizmannia.
OX NCBI_TaxID=1398;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 55055 / NEB 566;
RX PubMed=8276869; DOI=10.1016/s0021-9258(17)42403-3;
RA Kong H., Roemer S.E., Waite-Rees P.A., Benner J.S., Wilson G.G.,
RA Nwankwo D.O.;
RT "Characterization of BcgI, a new kind of restriction-modification system.";
RL J. Biol. Chem. 269:683-690(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RC STRAIN=ATCC 55055 / NEB 566;
RX PubMed=8451198; DOI=10.1093/nar/21.4.987;
RA Kong H., Morgan R.D., Maunus R.E., Schildkraut I.;
RT "A unique restriction endonuclease, BcgI, from Bacillus coagulans.";
RL Nucleic Acids Res. 21:987-991(1993).
RN [3]
RP NOMENCLATURE, AND SUBTYPES.
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 B, G, H and S subtype restriction enzyme that recognizes
CC the double-stranded sequence 5'-CGAN(6)TGC-3' and cleaves bilaterally
CC and symmetrically 10 base pairs upstream and 12 base pairs downstream
CC of the sequence to release a 34-base pair fragment. Methylation of the
CC recognition sequence occurs on the adenine in either one or both
CC strands; seems to methylate restricted DNA (PubMed:8451198,
CC PubMed:8276869, PubMed:12654995). This subunit has no methylation or
CC DNA restriction activity on its own (PubMed:8276869).
CC {ECO:0000269|PubMed:8276869, ECO:0000269|PubMed:8451198,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000269|PubMed:8451198};
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 Evidence={ECO:0000269|PubMed:8276869, ECO:0000269|PubMed:8451198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8451198};
CC -!- ACTIVITY REGULATION: DNA restriction requires S-adenosyl-L-methionine
CC and Mg(2+), and is inhibited by S-adenosyl-homocysteine
CC (PubMed:8451198). SAM may be a cofactor for DNA restriction (Probable).
CC {ECO:0000269|PubMed:8451198, ECO:0000305|PubMed:8451198}.
CC -!- SUBUNIT: Heterotrimer of two A and one B subunit. Both subunits are
CC necessary for DNA-binding, which is sequence non-specific.
CC {ECO:0000269|PubMed:8276869}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the N(4)/N(6)-
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; L17341; AAA16626.1; -; Unassigned_DNA.
DR PIR; A53125; A53125.
DR AlphaFoldDB; Q07605; -.
DR SMR; Q07605; -.
DR REBASE; 238; BcgI.
DR PRO; PR:Q07605; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW Methyltransferase; Multifunctional enzyme; Nuclease; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..637
FT /note="Type II restriction enzyme and methyltransferase
FT RM.BcgI"
FT /id="PRO_0000077378"
SQ SEQUENCE 637 AA; 71559 MW; 0ED5ABD934E85AAF CRC64;
MVNEKTSTDQ LVRRFIEDLG VTYEEQGSSN IQIKQALRSA SKSKSQSGVG KPEFIFFSGN
HLIIVEDKLA IDKLEYKNND GIIDTEFPFR RDYAVNGAVH YARHIIEKTN SYKEVIAIGI
AGDGLHYQIH PYFVSETELK KLPEMKSLED ISPENIEEFY KVAVLGELPK EERELREVNK
IAADMHEDLR NYGQLEGEKK ATVVSAILLA LEEPTFSLNQ LIGSDRVGGT DGEIIFNAVR
VYLENAGIVP YAKVGEMLDQ FIFIQRDVTL NTVNSNLEMT PLKYFATTLE AEIMDKIKSN
TDFDILGNFY GEFVKYGGND GNPLGIVLTP RHITSLMAEL IGINKSDFVL DPACGTGAFL
ISAMNRMLGQ AENDDERRDI KQNRLYGIEI QQKLFTIATT NMILRGDGKS NLIRDNCLTF
DNTIMNGYGI NKILMNPPYS QAKNDQTQHL SELSFIQQAL EMLVVGGKLC AIVPQSTMVG
KNRHDKARKK QILKQHTLET VITLNKDTFH GVGVNPCIVI FKAGIKHPEN KRVSFVNFED
DGHVVRKHVG LVGDGTEKGK REHLLAVLAG DEDDGTDLIV KTAIKDTDEW LHSFYYFNDG
IPSEDDFYKT VANYLTFQFD MTANGKGYLF EGVEENE
