ID   ADDB_BACC4              Reviewed;        1171 AA.
AC   B7HGP8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=BCB4264_A1192;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-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; CP001176; ACK60886.1; -; Genomic_DNA.
DR   RefSeq; WP_000058594.1; NZ_VEHB01000003.1.
DR   AlphaFoldDB; B7HGP8; -.
DR   SMR; B7HGP8; -.
DR   EnsemblBacteria; ACK60886; ACK60886; BCB4264_A1192.
DR   KEGG; bcb:BCB4264_A1192; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000007096; 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; 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..1171
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379157"
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;  134168 MW;  03219F867E04BF83 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
     TMREEMDEFE NYCLAYGVQG KRWTSEDPWM YRRYRSLDDT NGMITDSERE MEEKINRLRD
     VVRTPVIRMQ KRLKRAGTVM QMCEAVYLFL EELDVPKKLE ELRIRAEESG DFLFATDHEQ
     VWEEVMSLLD TFVEMLGEEK MSLSMFTDVM STGLEALQFA NIPPSLDQVL IANIDHSRLS
     DVKATFIIGV NEGVIPAAPM DEGMLSDEER EVLGAAGIEL APTTRQTLLE EQFVMYQMVT
     RASEKLYISC PLADEEGKTL LASSFIKKIK RMFPNVKDSF ITNDVNDLSR SEQISYVATP
     EVTLSYVMQQ LQTWKRYGFE GNLDFWWDVY NFYVTSDEWK QKSSRVLSSL FYRNRAKKLS
     TAVSRDLYGD IIKGSVSRME LFNRCAYAHF AQHGLSLRER DIFKLDAPDI GELFHAALKK
     IADKLLRENR TWADLSIKEC EHLSVLVIEE IAPLLQRQIL LSSNRHFYLK QKLQQIIFRT
     SIILREHAKS SGFVPVDLEV PFGMGGTGSL PPMEFSLPNG VKMEVVGRID RVDKAEDENG
     TFLRIIDYKS SSKVLDLTEV YYGLALQMLT YLDVVTSNAQ TWMKKGHAAS PAGVLYFHIH
     NPIVEMKGDA SEAEIEKEIL KKFKMKGLVL GDADVVRLMD NKLSTGSSDI ISAGLKKDGS
     FSARSSIASE QEFNVLQKYV HHTFENIGKD ITEGVIDIAP YKMGNKAACT FCNFKSVCQF
     DESLEDNQFR SLKDMKDSEA MEKIREEVGG E