ID   T4BB_WEICA              Reviewed;         341 AA.
AC   Q07606;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Type II restriction enzyme BgcI specificity subunit S.BcgI {ECO:0000303|PubMed:12654995};
DE            Short=S.BcgI;
DE            EC=3.1.21.4 {ECO:0000269|PubMed:8451198};
DE   AltName: Full=Restriction enzyme BgcI subunit B {ECO:0000303|PubMed:8276869};
GN   Name=bcgIB {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 1-18, FUNCTION, AND
RP   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, 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: The specificity subunit (PubMed:12654995). A B, G, H and S
CC       subtype restriction enzyme that recognizes the double-stranded sequence
CC       5'-CGAN(6)TGC-3' and cleaves bilaterally and symmetrically 10 base
CC       pairs upstream and 12 base pairs downstream of the sequence to release
CC       a 34-base pair fragment. Methylation of the recognition sequence occurs
CC       on the adenine in either one or both strands; seems to methylate
CC       restricted DNA (PubMed:8451198, PubMed:8276869, PubMed:12654995). This
CC       subunit degrades DNA in a non-specific manner (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   -!- 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: Belongs to the type-I restriction system S methylase
CC       family. {ECO:0000305}.
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DR   EMBL; L17341; AAA16627.1; -; Unassigned_DNA.
DR   PIR; B53125; B53125.
DR   AlphaFoldDB; Q07606; -.
DR   SMR; Q07606; -.
DR   REBASE; 4024; S.BcgI.
DR   PRO; PR:Q07606; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.220.20; -; 2.
DR   InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   Pfam; PF01420; Methylase_S; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW   Nuclease; Restriction system.
FT   CHAIN           1..341
FT                   /note="Type II restriction enzyme BgcI specificity subunit
FT                   S.BcgI"
FT                   /id="PRO_0000077379"
SQ   SEQUENCE   341 AA;  39161 MW;  E803D59E548AFD40 CRC64;
     MNNLIKYSTF LISDLFDVVI GKTIDGNKAQ RNENGTPYIT RKATRNGFEF MIDGEKEKLY
     SGKLPVITIG NETSKPFVQE FHFFTGTKVN ICIPKLDLNR NHLLYITTMI ENATKMFSYS
     YTINSTRLKS LKILLPIKGE EPDWDYMNTY ISKILSNMEK NFDVQQNDGV SDLRSLKDLS
     WSQFKMDEIF SINSGVRLTK ADMKPGNIPF IGATDSNNGI TEFTSSTNAS FDGNVLGVNY
     NGSVVENFYH PYKAVFSDDV KRLKLKNYPN NKHVLLFMKV VILQQKVKYA YGYKFNATRM
     KEQIILLPTK ADGTPDYEFM EQYMMRMENK VVGRTTEKEA D