ID   ADDB_BACCR              Reviewed;        1171 AA.
AC   Q81GQ0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BC_1137;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08124.1; -; Genomic_DNA.
DR   RefSeq; NP_830923.1; NC_004722.1.
DR   RefSeq; WP_000058591.1; NC_004722.1.
DR   AlphaFoldDB; Q81GQ0; -.
DR   SMR; Q81GQ0; -.
DR   STRING; 226900.BC_1137; -.
DR   EnsemblBacteria; AAP08124; AAP08124; BC_1137.
DR   KEGG; bce:BC1137; -.
DR   PATRIC; fig|226900.8.peg.1100; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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; 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;
KW   Reference proteome.
FT   CHAIN           1..1171
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379156"
FT   DOMAIN          1..390
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;  134145 MW;  DEA299A242282036 CRC64;
     MSLRFVIGRA GSGKSTLCLR EVQEELKQRP RGKTILYLVP EQMTFQTQQA LIGSEDVRGS
     IRAQVFSFSR LAWKVLQEVG GASRLHIDEA GVHMLLRKIV ESRKDGLSVF QKAAEQNGFF
     EHLGSMIAEF KRYNVTPSNV YEMWQQLDAH SSSAEQKLLA NKVYDLQLLY DDFERALIGK
     YLDSEDYLQL LVEKLPQSEY VNGAEIYIDG FHSFSPQELE IVRQLMICGA RVTITLTIDE
     KTLAQPVNEL DLFYETTLTY EKIKQVAREE KIEIEKTIPL MEQPRFHSPA LAHLEAHYEA
     RPNEKFNGEA SVTISTAANL RAEVEGVARE IRKLVADEKY RYRDIAVLLR NGESYYDVMR
     TLFTDYNIPH FIDEKRPMSH HPLVECIRSA LEIISGNWRY DAVFRCVKTE LLYPLDVRKE
     AMREEMDEFE NYCLAYGVQG KRWTAEDPWM YRRYRSLDDT NGMITDSERE MEEKINRLRD
     VVRTPVIRMQ KRLKRAGTVM QMCEAVYLFL EELDVPKKLE ELRIRAEESG DFLFATDHEQ
     VWEEVMSLLD TFVEMLGEEK MSLSMFTDVM STGLEALQFA NIPPSLDQVL IANIDHSRLS
     DVRATFIIGV NEGVIPVAPM DEGMLSDEER EVLGAAGIEL APTTRQTLLE EQFVMYQMVT
     RASEKLYISC PLADEEGKTL LASSFIKKIK RMFPNVKDSF ISNDVNDLSR SEQISYVATP
     EVTLSYVMQH LLTWKRYGFE GNLDFWWDVY NFYVTSDEWK QKSSRVLSSL FYRNRAKKLS
     TAVSRDLYGD IIKGSVSRME LFNRCAYAHF AQHGLSLRER DIFKLDAPDI GELFHAALKK
     IADKLLRENR TWADLSIKEC EHLSVLVIEE IAPLLQRQIL LSSNRHFYLK QKLQQIIFRT
     SIILREHAKS SGFVPVDLEV PFGMGGTGSL PPMEFSLPNG VKMEVVGRID RVDKAEDENG
     TFLRIIDYKS SSKALDLTEV YYGLALQMLT YLDVVTSNAQ TWMKKGHAAS PAGVLYFHIH
     NPIVEMKGDA TEAEIEKEIL KKFKMKGLVL GDADVVRLMD NKLSTGSSDI ISAGLKKDGS
     FSARSSIASE QEFNVLQKYV HHTFENIGKD ITEGVIDIAP YKMGNKAACT FCNFKSVCQF
     DESLEDNQFR SLKDMKDSEA MEKIREEVGG E