ID   ADDB_CLOB8              Reviewed;        1159 AA.
AC   A6LPC3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Cbei_0013;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) 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; CP000721; ABR32203.1; -; Genomic_DNA.
DR   RefSeq; WP_011967378.1; NC_009617.1.
DR   AlphaFoldDB; A6LPC3; -.
DR   SMR; A6LPC3; -.
DR   STRING; 290402.Cbei_0013; -.
DR   PRIDE; A6LPC3; -.
DR   EnsemblBacteria; ABR32203; ABR32203; Cbei_0013.
DR   KEGG; cbe:Cbei_0013; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000565; 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   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF52980; SSF52980; 1.
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..1159
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379168"
FT   DOMAIN          1..401
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          279..582
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         787
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   1159 AA;  135060 MW;  8952F5AD8CFA98E4 CRC64;
     MSIRFVYGRS GTGKSKFCID EIKNNIDKKL DFNKLILLVP EQYTFMTENK ILHEIGENAF
     FRTEVLSFKK MAHNIFEEYG GRVKEIIKES GRNMLIHRVI NENIEFLDYF NRMSREQGFN
     EIISEVISEF KKYNISIDSI RAIDEKINDA ELYQKVKELM IIYEAFNLKM HENYIDGDDE
     LTLLDKKLLE SSAYVDSEVW IDEFTSFTPQ QLDIIKVLAK RCRRVNITFC IDNKSLNNNS
     EDITDVFNII KSTENKILKI MKENNIAYDK PVNLNNAIPY RFKGNLELDH IEKYFFSYPF
     NEYDKNPESI TLYKASNIYD EIERVSKSIT SLVRENGYRY RDISVVCRNI DDYEKIISVI
     FKDYNIPYFL DKKIQLLSNP LIVLISSAFE ILLKNWSYES VFKYLKSGLT GIDNSYIDRL
     ENFILEYGVK GYKWTSKEIV NEKWFRGNGE LTDDKVLIAE IMEEIRYPLM TFHNKVNGKH
     KVKDICSAIY EFLVDVKVFD RINEWIKNFE ELGLEDKVKE YSQVESIVID IIDQAVDVIG
     EERLEYSEFF RILSSGFANE EIGIIPVALD QVNIGDIARI KGRDVKVLYI VGINDGVLPA
     SKKEEGLLSD RDRTTLGEVG INLSSTTRNK VFEEQYLLYM ALTISSEYLM LSYPMADFEG
     KSLRPSIVIS RIKKIFPNLI EESAIYDLKI LENKFGKIIA PIPTFNELII SMRKDFDKEY
     IEPYWSEVYE WFKNNDEFRD KVKNIFKGLS YSNIGDKVSK NKLRKLYQND LEKLVFSVSK
     LEKYAECPFS YFVQYGLKAK NRKVYEFTPP DLGSFVHEML DSFTNKVRED GVLWSDLSNE
     KCKEIISNLI DKKLMDESNS ILNSTKKFKY LAQRFKRVIS KSVSVIASQI GKGEFEVFKT
     EFDFGSYSSG EAITLDLNDN EKVYLQGRID RIDKLDLDGE TYIRIIDYKT GAKKFDLNEI
     YYGLQVQLLV YLDALIKNSK YILDKQVKPG AILYFKIDDP IIKSKKEMTD EEVEKEVLSA
     LKMKGLVLKD ARVVKAMDKD IEGYSLVIPA SFKADGGFKA TSDVVTEEEF RILREYVNRK
     MIEICEEMLS GDIKIQPTKN SNIAHCEYCD FSSICQFDTE IKDNKYKIII NKSTNDIWNN
     IKKEIDNSNK LIKVENEEV