ID   B1KV90_CLOBM            Unreviewed;       916 AA.
AC   B1KV90;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE            Short=R protein {ECO:0000256|RuleBase:RU364115};
DE            EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
DE   AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN   OrderedLocusNames=CLK_1539 {ECO:0000313|EMBL:ACA55536.1};
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA55536.1, ECO:0000313|Proteomes:UP000000722};
RN   [1] {ECO:0000313|EMBL:ACA55536.1, ECO:0000313|Proteomes:UP000000722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC       activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC         fragments with terminal 5'-phosphates, ATP is simultaneously
CC         hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851,
CC         ECO:0000256|RuleBase:RU364115};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000256|ARBA:ARBA00011296,
CC       ECO:0000256|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC       ECO:0000256|RuleBase:RU364115}.
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DR   EMBL; CP000962; ACA55536.1; -; Genomic_DNA.
DR   RefSeq; WP_012343505.1; NC_010520.1.
DR   AlphaFoldDB; B1KV90; -.
DR   REBASE; 17443; CboA3ORF1538P.
DR   KEGG; cbl:CLK_1539; -.
DR   HOGENOM; CLU_004848_1_0_9; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR   Gene3D; 3.90.1570.50; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   InterPro; IPR022625; TypeI_RM_Rsu_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
DR   PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR   Pfam; PF12008; EcoR124_C; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF18766; SWI2_SNF2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364115};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          254..403
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   916 AA;  107404 MW;  8504D735F452940C CRC64;
     MAYQSEAELE KQLIKQLESK GYNKVKISTE EELIKNFRVQ LNKYNEEKLA GTPLTDKEFE
     RVMRKVEGKS IFEGAKILRD KWPLKRDDGL EVYIEFFNSK SLCKNIFQVT TQTTVVGKYT
     NRYDVTLLVN GLPLVQIELK RRGVDFKEAF NQIQRYRKHS YQGLYRYIQI FIVSNGMDTK
     YFSNSDRDIL YTHTFFWTDE KNQRISKLND FTDTFLERSF ISKIIARYMI INYTEKILMV
     MRPYQIYAVE ALINRALETN GNGYIWHTTG SGKTLTSFKA SQILSKEPKI KKVFFLVDRK
     DLDSQTINEF NKFEPKSVDV TDKTSTLIKQ IKDVNKPLIV TTIQKMANAI KSPRYTKIME
     QYKDEKVAFI IDECHRSQFG SMHIAIEKHF KKAQYFGFTG TPILKENKSQ DGRTTADLFD
     EMLHSYLIKD AIKDNNVLGF SVEYISTFKG QFDENDDTKV KAIDKKEAFM DDERISQIAQ
     DIIKNHNKKT KDRQYTAIFA VESIEMLVKY YDKFKKLDHN LKITGIFSYG VNEDAEGKDE
     HSRDSLEEII KDYNEMFDTK YSTDTFQGYF ANVSKKVKSG QIDILIVVNM FLTGFDSKTL
     NTLYIDKNLA YHSLIQAYSR TNRVYKSTKP YGNIVCYRNL KKKTDEAIKL FSLTDNANEV
     LMKSYNHYLE AFKESVLNLY KIVPRPEDVD FIEGEKEKKE FIVAFRELSK ILIKLQTFVE
     FEFDEDKLLI SEQTYQDFKS KYLAIYDSFK NDEEGKASIL DDIDFGIELM HTDKINVDYI
     MNLIRNIDFS DKENKEKDIK HIIKELDRAD SEHLRLKVDL LKSFLQEVVP NLTEEDSIDD
     AYSRFEQVQR TEEIKAFSEQ AAVKEGKLKD YISEYEYSGM LDRKDMGDTI EGSFLKRKKV
     VNKITTFIKN HVEKFS
//