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 27-MAR-2024, entry version 84.
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 AltName: Full=ATP-dependent helicase/nuclease subunit 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; Bacillota; 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 subunit has 5' -> 3'
CC nuclease activity but not helicase activity. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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 -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- MISCELLANEOUS: Despite having conserved helicase domains, this subunit
CC does not have helicase activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01452}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000227; ACM11630.1; -; Genomic_DNA.
DR AlphaFoldDB; B9ITE8; -.
DR SMR; B9ITE8; -.
DR KEGG; bcq:BCQ_1200; -.
DR HOGENOM; CLU_007838_0_0_9; -.
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-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 3.90.320.10; -; 1.
DR Gene3D; 6.10.140.1030; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR049035; ADDB_N.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR NCBIfam; TIGR02773; addB_Gpos; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF21445; ADDB_N; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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; DNA-binding; Exonuclease;
KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW 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
//
