ID   ADDB_CLOBB              Reviewed;        1152 AA.
AC   B2THC7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=CLL_A0024;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC       and an ATP-dependent, dual-direction single-stranded exonuclease.
CC       Recognizes the chi site generating a DNA molecule suitable for the
CC       initiation of homologous recombination. The AddB nuclease domain is not
CC       required for chi fragment generation; this subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
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DR   EMBL; CP001056; ACD22230.1; -; Genomic_DNA.
DR   RefSeq; WP_012423101.1; NC_018648.1.
DR   AlphaFoldDB; B2THC7; -.
DR   SMR; B2THC7; -.
DR   EnsemblBacteria; ACD22230; ACD22230; CLL_A0024.
DR   KEGG; cbk:CLL_A0024; -.
DR   PATRIC; fig|935198.13.peg.15; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 3.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1152
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379171"
FT   DOMAIN          1..338
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          276..579
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         785
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1106
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1109
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1115
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1152 AA;  133899 MW;  66834174BEE232A4 CRC64;
     MSIRFIYGRA GSGKSLFCIN QIKKLIDSDK EKKIILLVPE QYTFTTENKV LNHIGERAAL
     NTHVLSFRTM CQKVFEECGG RVKQIIKDTG KHMLINKVLN EKIDDLSYFK KMSREQGFNN
     IISELITEFK KYNIDIDALR DLTDKIDDNE LVEKIRELSL IYEEFNVKMH SSYIDTDDEL
     TLLAKKLLAN NIYANSEIWI DEFTTFTPQQ LEIIRIISKT SVVNITLCMD KIENSDAEDI
     TNVFSSIENT ENRILKLMEE NNIGYLNPIN LNSKLPYRFK NSEELAHIEK YCITYPFKSY
     KGKNKDVRLY KANNTYDEIE KVAQDIIRLV RDRNYRFRDI SVVCRNIEDY NKIISVIFND
     YEIPFFMDKK IKLLNNPLII LITSAFEVLL KNWSYESVFK YLKSGLTGFN TYDIDRLENF
     VLEHGIKSYK WNEEEIKKLK NISIENGATE EELTIFNVME EVRNSLISFH KLIEGKHNVR
     DICKALYEFL LSIKAFERID EWIIKFEELK LEDKVKEYKQ VESIVIDMLD QAVEVMGSDV
     VDTFEFFKIL NSGFENEEIG VIPVALDQVN VGDIARIKGR EVKALYIVGI NDGILPAAHK
     DEGILSDRDR IELKEFGVVL AADGRSKAFE EQFVVYTALT IASEYLMLSY PMADFEGKSL
     RPSIIISRIK KILPNLVEES SLYDLSKGND HFNKVISPIP TFNELIFALR RELEDEEIDE
     EYWGEVYNWF KENEDFKWKI ENIFKGLRYS NTGEKVSRNK LLSLYKNDLG KLSFSVSRLE
     KYAECPFSYF IQYGLKAKNR KVYEFTPPDL GSFVHDILDS FTNKVKKEKI AWSDLDMIKC
     KNIVSELIDT KLKEDSGSIL NSTNKYKYFS KRFKRVISKS VSVISEQMRR GEFEVFNNEF
     SFGSYNDGEA IVLELPSNEK VYLNGRIDRI DTLDLEGSTY LRIVDYKTGN KHFDLNEFYY
     GLQMQLLVYL DALLKNSEYI LKKQALPGAV LYFRVDDPII KTKGDITTEE LEKEVLSNLK
     MNGLILKDAK VVKAMDRGIE TDGYSLVIPA ALKKDGDFKA GSEVVTEEQF NLLREYVNKK
     MIDLCEDMLC GDIKIQPTKD SDGSHCEFCD FSSICQFDSS IEDNKYKIIM KKSKDEIWNN
     IRDELNDDKK EN