ID   ADDB_CLOBA              Reviewed;        1152 AA.
AC   B2UX56;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CLH_0024;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
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 genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-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; CP001078; ACD52231.1; -; Genomic_DNA.
DR   RefSeq; WP_012450421.1; NC_010723.1.
DR   AlphaFoldDB; B2UX56; -.
DR   SMR; B2UX56; -.
DR   KEGG; cbt:CLH_0024; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
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_0000379169"
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;  134107 MW;  075319C09F583412 CRC64;
     MSIRFIYGRA GSGKSLFCIN QIKKLIDSDK EKKIILLVPE QYTFTTENKV LNYIGERAFL
     NTHVLSFRTM CQKVFEECGG RVKQIIKDTG KHMLINKVLN EKIDDLSYFK KMSREQGFNN
     IISELITEFK KYNINIDALR DLTDKIDDNE LVEKIRELSL IYEEFNVKMH SSYIDTDDEL
     TLLAKKLLAN NIYANSEIWI DEFTTFTPQQ LEIIRILSKA SVVNITLCMD KIENSDVEDI
     TNVFSSIENT ENRLLKLMEE NNIGYLNPIN LNSKLPYRFK NSEELSHIEK YCITYPFKSY
     KGKNKDVRLY KANNTYDEIE KVAKDIIRLV RDRNYRFRDI SVVCRNIENY NKIISVIFND
     YEIPFFMDQK IKLLNNPLIV LITSAFEVVL KNWSYESVFK YLKSGLTGFN IYDIDRLENF
     VLEHGIKSYK WNEEEIEKLK NIKIENGATE DELTIFNLME EVRNSLISFH KLIEGKHYVR
     DICKALYEFL LSIKAFERID EWIIKFEELK LEDKVKEYKQ VESIVIDMLD QAVEVMGSDV
     VDTFEFFKIL NSGFENEEIG VIPVALDQVN VGDIARIKGR EVKALYIVGI NDGILPAAHK
     DEGILSDRDR IELKEFGIVL AADGRSKAFE EQFVVYTALT IASEYLMLSY PMADFEGKSL
     RPSIIISRIK KILPNLVEES SLYDLSKRSD HFNKVISPIP TFNELIFALR RELEDEDIDE
     EYWGEVYNWF KENEDFKWKI ENTFKGLRYS NTGEKVSRNK LLSLYKNDLG KLSFSVSRLE
     KYAECPFSYF IQYGLKAKNR KVYEFTPPDL GSFVHDILDS FTNKVKKEKI AWSDLDMIKC
     KNIVSELIDT KLKEDSGSIL NSTNKYKYFS KRFKRVISKS VSVISEQMRR GEFEVFNNEF
     SFGSYNDGEA IVLELPSNEK VYLNGRIDRI DTLDLEGSTY LRIVDYKTGN KHFDLNQFYY
     GLQMQLLVYL DALIKNSEYI LKKQALPGAV LYFKVDDPII KTKGDITTEE LEKEVLSNLK
     MNGLILKDAK VVKAMDRGIE TDGYSLVIPA ALKKDGDFKA GSEVVTEEQF TLLREYVNKK
     MIDLCEDMLC GDIKIQPTKD SDGSHCEFCD FSSICQFDSS IEDNKYKIIM KKSKDEIWNN
     IRDELNDDKK EN