ID ADDB_BACMK Reviewed; 1171 AA.
AC A9VJ01;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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};
GN OrderedLocusNames=BcerKBAB4_1040;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
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 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}.
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DR EMBL; CP000903; ABY42290.1; -; Genomic_DNA.
DR RefSeq; WP_012260537.1; NC_010184.1.
DR AlphaFoldDB; A9VJ01; -.
DR SMR; A9VJ01; -.
DR KEGG; bwe:BcerKBAB4_1040; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR Proteomes; UP000002154; 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_0000379166"
FT DOMAIN 1..301
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; 134314 MW; 4BD5C19CFFA15DD7 CRC64;
MSLRFVIGRA GSGKSTLCLH EVQEELKQRP RGKTILYLVP EQMTFQTQQA LIGSEDVRGS
IRAQVFSFSR LAWKVLQEVG GASRLHIDEA GVHMLLRKIV ESRKDGLSVF QKAAEQNGFF
EHLGSMIAEF KRYNVTPSNV YEMWQQLDTH SSSAEQKLLA NKVYDLQLLY DDFERALIGK
YLDSEDYLQL LIEKLSDSEY VKGAEIYIDG FHSFSPQELE IVRGLMRLGT RVTITLTIDE
KTLAQPVNEL DLFYETTLTY ERIKQVAREE KIEVEKTIPL MKQPRFHSQA LAHLEMHYEA
RPNEKFHGEA SVTISTAANL RAEVEGVARE IRRLVATEDY RYRDIAVLLR NGESYYDVMR
TLFTDYNIPH FIDEKRPMSH HPLVECIRSA LEIISGNWRY DAVFRCVKTE LLYPLDVRKE
AMREEMDEFE NYCLAYGVQG KRWTSEDPWM YRRYRSLDDA SEMITDSERE MEEKINRLRD
VVRTPVIRMQ KRLKRAGTVM QMCEAVYLFL EELDVPKKLE ALRIRAEESG DFLFATDHEQ
VWEEVMSLLD TFVEMLGEEK MSLSMFTDVM TTGLEALQFA NIPPSLDQVL VANIDHSRLS
DIKATFIIGV NEGVIPAAPM DEGMLSDEER NVLTAAGIEL APTTRQTLLE EQFVMYQMVT
RASEKLYISC PLADEEGKTL LASSFIKKIK RMFPDVKESF ITNDVNDLSR SEQLSYVATP
EVTLSYVMQQ LQTWKRYGFE GNLDFWWDVY NFYVTSDEWK QKSSRVLSSL FYRNRAQKLS
TDVSRDLYGD TIKGSVSRME LFNRCAYAHF AQHGLSLRER DIFKLDAPDI GELFHAALKR
IADKLLRENR TWADLSIKEC EHLSALVIEE IAPLLQRQIL LSSNRHFYLK QKLQQIIFRT
SLILREHAKS SGFVPVDLEV PFGMGGTGSL PPMEFALPNG VKMEVVGRID RVDKAEDESG
TFLRIIDYKS SSKALDLTEV YYGLALQMLT YLDVVTSNAH TWMKKGSTAS PAGVLYFHIH
NPIVEMKGDA SEEEIEKEIL KKFKMKGLVL GDADVVRLMD NKLSTGSSDI ISAGLKKDGS
FSARSSIASE QEFNVLQKYV HHSFENIGKD ITEGVIDIAP YKKGNKAACT FCNFKSVCQF
DESLEDNQFR TLKDMKDSEA MEKIREEVGG E
//
