ID   ADDB_BACCQ              Reviewed;        1171 AA.
AC   B9ITE8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=BCQ_1200;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM11630.1; -; Genomic_DNA.
DR   RefSeq; WP_000058550.1; NC_011969.1.
DR   AlphaFoldDB; B9ITE8; -.
DR   SMR; B9ITE8; -.
DR   PRIDE; B9ITE8; -.
DR   EnsemblBacteria; ACM11630; ACM11630; BCQ_1200.
DR   KEGG; bcq:BCQ_1200; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000000441; 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; -; 4.
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..1171
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379159"
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   1171 AA;  134101 MW;  DA8469462F4DA43C CRC64;
     MSLRFVIGRA GSGKSTLCLH EVQEELKQRP RGETILYLVP EQMTFQTQQA LIGSEDVRGS
     IRAQVFSFSR LAWKVLQEVG GASRLHIDEA GVHMLLRKIV ESRKDGLSVF QKAAEQNGFF
     EHLGSMIAEF KRYNVTPSNV YEMWQQLDAH SSSAEQKLLA NKVYDLQLLY DDFERALIGK
     YLDSEDYLQL LVEKLPQSEY VKGAEIYIDG FHSFSPQELE IVRQLMICGA RVTITLTIDE
     KTLAQPVNEL DLFYETTLTY EKIKQVAREE KIEIEKTIPL MEQPRFHSPA LAHLEAHYEA
     RPNEKFNGEA SVTIHTAANL RAEVEGVARE IRRLVADENY RYRDIAVLLR NGESYYDVMR
     TLFTDYNIPH FIDEKRPMSH HPLVECIRSA LEIISGNWRY DAVFRCVKTE LLYPLDVRKE
     TMREEMDEFE NYCLAYGVQG KRWTSEDPWM YRRYRSLDDT DGMITDSERE MEEKINRLRG
     VVRTPVIRMQ KRLKRAGTVM QMCEAVYLFL EELDVPKKLE ALRIRAEESG DFLFATDHEQ
     VWEEVMSLLD TFVEMLGEEK MSLSMFTDVM STGLEALQFA NIPPSLDQVL IANIDRSRLS
     NVKATFVIGV NEGVIPAAPM DEGMLSDEER DVLSAAGIEL APTTRQTLLE EQFVMYQMVT
     RATEKLYISC PLADEEGKTL LASSFIKKIK RMFPDVKDTF ITNDVNDLSR SEQISYVATP
     EVTLSYVMQQ LQTWKRYGFE GNLDFWWDVY NFYVTSDEWK QKSSRVLSSL FYRNRAQKLS
     TAVSRDLYGD KIKGSVSRME LFNRCAYAHF AQHGLSLRER DIFKLDAPDI GELFHAALKR
     IADRLLRENR TWADLSIKEC EHLSAVVIEE IAPLLQRQIL LSSNRHFYLK QKLQQIIFRT
     SIILREHAKS SGFVPVDLEV PFGMGGTGSL PPMEFSLPNG VKMEVVGRID RVDKAEDENG
     TFLRIIDYKS SSKALDLTEV YYGLALQMLT YLDVVTSNAH TWMKKGGTAS PAGVLYFHIH
     NPIVEVKGDA SEAEIEKEIL KKFKMKGLVL GDADVVRLMD NKLSTGSSDI ISAGLKKDGS
     FSARSSIASE QEFNVLQKYV HHTFENIGKD ITEGVIDIAP YKKGNKAACT FCNFKSVCQF
     DESLEDNQFR TLKDMKDSEA MEKIREEVGG E