ID   ADDB_BACCN              Reviewed;        1170 AA.
AC   A7GM36;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Bcer98_0859;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS21194.1; -; Genomic_DNA.
DR   RefSeq; WP_011983948.1; NC_009674.1.
DR   AlphaFoldDB; A7GM36; -.
DR   SMR; A7GM36; -.
DR   STRING; 315749.Bcer98_0859; -.
DR   EnsemblBacteria; ABS21194; ABS21194; Bcer98_0859.
DR   GeneID; 56416446; -.
DR   KEGG; bcy:Bcer98_0859; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000002300; 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   Pfam; PF13361; UvrD_C; 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..1170
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379161"
FT   DOMAIN          1..343
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          281..587
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         805
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1129
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1132
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1138
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1170 AA;  134521 MW;  84B8617995F36D58 CRC64;
     MSLRFVIGRA GSGKSTLCLR EVQEELKERP RGKTILYLVP EQMTFQTQQA LIGSEEVRAS
     IRAQVFSFSR LAWKVLQEVG GASRLHIDEA GVHMLLRKII ESRKEGLYVF QKAAEQNGFF
     EHLGGMIAEF KRYNITPSHV YEMWQQLDAH SSSAEQKLLA NKIYDLQLLY DDFERALIGK
     YLDSEDYLQL LIEKLPFSEY VKDAEIYIDG FHSFSPQELE IIRQLMRCGA RMTITLTVDE
     KTFAQPVNEL DLFYETVLTY EKVKQVAREE KVVMEKTISL VEQPRFHSPA LAHLEAHYES
     RPNEKFYGET SIAIHTAANL RAEVEGVARE IRRLVAEENY RYRDIAVLLR NGESYYDVLR
     TLFADYDIPH FIDEKRSMSH HPLVECIRSA LEIISGNWRY DAVFRCVKTE LLYPLDVKKE
     VMREEMDEFE NYCLAYGVQG KKWTADEPWT YRRYRSLDEG NEVITDRERQ MEEKMNRLRE
     IVRTPIIRLQ KRLKRASTVM QMCEAVYLFL EELDVPKKLE QLRVRAEESG DFLFATDHDQ
     VWEEVMNLLD TFVEMLGEES MSLSVFIDVM TTGLEALQFA NIPPSLDQVL IANIDRSRLS
     NIRATFVIGA NEGVMPATPT DEGMLSDEER DVLAAAGVEL APTTRQTLLE EQFVLYQMVT
     RASEKLYISC PLADEEGKTL LASSFMKKIK RMFPNVKETF VTNDVNDLSR AAQISYVTTP
     EVTLSYVMQQ LQTWKRYGFE GDLDFWWDVY NFYVTSDEWK QKSNRVLSSL FYRNRAKKLS
     TAVSRILYGD KIKGSVSRME LFNRCAYAHF AQHGLSLRER DIFKLDAPDI GELFHAALKK
     IADKLLREKR TWADLSIKEC EHLSILVIEE IAPLLQRQIL LSSNRHAYLK QKLQQIIFRT
     SLVLREHAKA SGFVPVDLEV PFGMGGKDSL PPMEFTLSNG VKMEVVGRID RVDKAEDESG
     TFLRIIDYKS SSKALDLTEV YYGLALQMLT YLDVVISNAG TWMKQGEVAS PAGVLYFHIH
     NPLVEVKGDA SEEEIEKEIL KKFKMKGLVL GDADVVRLMD NKLSTGSSDI ISAGLKKDGS
     FSARSNIASE QEFSVLQKYV HHTFETIGKD ITEGVIDIAP YKMGNKAACT FCHFRSVCQF
     DESLEDNQFR TLKDMKDSEA MEKIREEVGE