ID   T3RE_BACC1              Reviewed;         987 AA.
AC   P25241; Q9XBI5;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Type III restriction-modification enzyme BceSI Res subunit {ECO:0000303|PubMed:12654995};
DE            EC=3.1.21.5;
DE   AltName: Full=Type III restriction enzyme BceSI {ECO:0000303|PubMed:12654995};
DE   AltName: Full=Type III restriction-modification enzyme Bce10987IP Res subunit;
GN   Name=res; Synonyms=t3res {ECO:0000303|PubMed:10217496};
GN   OrderedLocusNames=BCE_1019;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=10217496; DOI=10.1099/13500872-145-3-621;
RA   Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B.;
RT   "Genome organization is not conserved between Bacillus cereus and Bacillus
RT   subtilis.";
RL   Microbiology 145:621-631(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 410-821.
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=1587478; DOI=10.1016/0378-1119(92)90722-2;
RA   Hegna I.K., Karlstroem E.S., Lopez R., Kristensen T., Kolstoe A.-B.;
RT   "A type-III DNA restriction and modification system in Bacillus cereus?";
RL   Gene 114:149-150(1992).
RN   [4]
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 type III restriction enzyme that recognizes 2 inversely
CC       oriented double-stranded sequences 5'-CGAAG-3' and cleaves 25-27 base
CC       pairs downstream. After binding to one recognition site undergoes
CC       random one-dimensional diffusion along DNA until it collides with a
CC       stationary enzyme bound to the second DNA site, which is when DNA
CC       cleavage occurs. DNA restriction requires both the Res and Mod subunits
CC       (By similarity). {ECO:0000250|UniProtKB:Q5ZND2,
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=3.1.21.5;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000250|UniProtKB:P08764};
CC   -!- SUBUNIT: Contains two different subunits: Res and Mod.
CC       {ECO:0000250|UniProtKB:Q5ZND2}.
CC   -!- SIMILARITY: Belongs to the type III restriction-modification system Res
CC       protein family. {ECO:0000305}.
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DR   EMBL; AJ007510; CAB40612.1; -; Genomic_DNA.
DR   EMBL; AE017194; AAS39950.1; -; Genomic_DNA.
DR   EMBL; X60713; CAA43125.1; -; Genomic_DNA.
DR   PIR; S15518; JC1116.
DR   RefSeq; WP_000698184.1; NC_003909.8.
DR   AlphaFoldDB; P25241; -.
DR   SMR; P25241; -.
DR   REBASE; 2841; BceSI.
DR   EnsemblBacteria; AAS39950; AAS39950; BCE_1019.
DR   GeneID; 59158737; -.
DR   KEGG; bca:BCE_1019; -.
DR   HOGENOM; CLU_011799_1_0_9; -.
DR   OMA; ELWQTIN; -.
DR   BRENDA; 3.1.21.5; 648.
DR   PRO; PR:P25241; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015668; F:type III site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR045572; RE_endonuc_C.
DR   InterPro; IPR014883; VRR_NUC.
DR   Pfam; PF19778; RE_endonuc; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00990; VRR_NUC; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Helicase; Hydrolase; Nuclease;
KW   Nucleotide-binding; Restriction system; S-adenosyl-L-methionine.
FT   CHAIN           1..987
FT                   /note="Type III restriction-modification enzyme BceSI Res
FT                   subunit"
FT                   /id="PRO_0000077376"
FT   DOMAIN          886..974
FT                   /note="VRR-NUC"
FT                   /evidence="ECO:0000255"
FT   REGION          50..545
FT                   /note="Helicase-like domain"
FT                   /evidence="ECO:0000250|UniProtKB:P08764"
FT   REGION          915..939
FT                   /note="Endonuclease domain"
FT                   /evidence="ECO:0000250|UniProtKB:P08764"
FT   CONFLICT        410..462
FT                   /note="TFERLLKEKLSRLVAEYEFKRLPREKEYLEFLRATQSSLASDNQNVHAGYFG
FT                   E -> GDYQFIETKAPTGYDLNAKPIPFTITKGQAQVTSVTALNSLTTGSMELMKVDM
FT                   (in Ref. 3; CAA43125)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   987 AA;  114787 MW;  1D0D6CF4112407FC CRC64;
     MKILLEELPH QEESLKAILE NFTGIDNAAN DSDVDYVYAN PLIRGRYNEI SNIDVKMETG
     TGKTYVYTRL MYEMHQQYGI FKFVIVVPSP AIKEGAKNFI QSDYAKQHFS QFYENVRIEL
     NVINAGDFKS KSGRRNFPAQ LLNFVEGSRQ NSNTIEVLLI NADMLRSKSM RNNDYDQTLI
     GGTTSPIEAI QDTRPVVIID EPHRFPRDKA NYQSIEAIKP QVIIRFGATF PEVTTGKGSN
     KITKKDYYRK KPQFDLNAIE SFNNGLVKGI DIYYPNLTEE QAKNRYVVDS VKAKELVLKQ
     NSKSWILHVG DNLAEVDSGF EGDIEYAGSK MLSNELELEK GMTLIPGTYR STYQELIIKD
     AIDKHFEIEQ ANFLRANQRE NNVPRIKTLS LFFIDSITSY RQDDGWLKAT FERLLKEKLS
     RLVAEYEFKR LPREKEYLEF LRATQSSLAS DNQNVHAGYF GEDRGSGDES IQAEVDDILK
     NKEKLLSFKD ENGNWQTRRF LFSKWTLREG WDNPNVFVIA KLRTSGSDNS KIQEVGRGLR
     LPVDETGHRI QQDEWPTRLA FLIGYDEKDF AQKLIGEINS DAKLQLNEEK LTEDMIQLIV
     TKRKKVNPEF TDERLLEHLD NLGIINRKNE FKESIDIGGV QKSGFEWLVE LYPELNTNRL
     REGKVIDTKK HSIKVRVKLR KENWEKVKEL WQQFSNRYML EFQRIPETIS FMAEQIVGNH
     SLYEREVPMQ MKESLHASDD NESVVLREQE NEYQRIYLPG MAYGKFVKRI NIATGIPIKE
     IHANLFKLMK SSLKGDARYL SELSLNNIIR EFKKRFDEIF AQAYEYKKLD FQARTAIYNP
     EMDSFVDDIN AEVIGVNIDE QAQEDNRYLY ELPPMRYDSV TPERDLLRHG YNDKVTVFGK
     LPRRAIQVPK YTGGSTTPDF IYMIEKDNDS SVYVLVETKA ENMRLEDQRI IDIQKKFFDT
     LKEHHIEFIE ATSAQQVYSI IRKLSEE