ID ADDB_CLOBB Reviewed; 1152 AA.
AC B2THC7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=CLL_A0024;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-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 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; CP001056; ACD22230.1; -; Genomic_DNA.
DR AlphaFoldDB; B2THC7; -.
DR SMR; B2THC7; -.
DR KEGG; cbk:CLL_A0024; -.
DR PATRIC; fig|935198.13.peg.15; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR Proteomes; UP000001195; 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; 3.
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 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..1152
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379171"
FT DOMAIN 1..338
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 276..579
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 785
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1152 AA; 133899 MW; 66834174BEE232A4 CRC64;
MSIRFIYGRA GSGKSLFCIN QIKKLIDSDK EKKIILLVPE QYTFTTENKV LNHIGERAAL
NTHVLSFRTM CQKVFEECGG RVKQIIKDTG KHMLINKVLN EKIDDLSYFK KMSREQGFNN
IISELITEFK KYNIDIDALR DLTDKIDDNE LVEKIRELSL IYEEFNVKMH SSYIDTDDEL
TLLAKKLLAN NIYANSEIWI DEFTTFTPQQ LEIIRIISKT SVVNITLCMD KIENSDAEDI
TNVFSSIENT ENRILKLMEE NNIGYLNPIN LNSKLPYRFK NSEELAHIEK YCITYPFKSY
KGKNKDVRLY KANNTYDEIE KVAQDIIRLV RDRNYRFRDI SVVCRNIEDY NKIISVIFND
YEIPFFMDKK IKLLNNPLII LITSAFEVLL KNWSYESVFK YLKSGLTGFN TYDIDRLENF
VLEHGIKSYK WNEEEIKKLK NISIENGATE EELTIFNVME EVRNSLISFH KLIEGKHNVR
DICKALYEFL LSIKAFERID EWIIKFEELK LEDKVKEYKQ VESIVIDMLD QAVEVMGSDV
VDTFEFFKIL NSGFENEEIG VIPVALDQVN VGDIARIKGR EVKALYIVGI NDGILPAAHK
DEGILSDRDR IELKEFGVVL AADGRSKAFE EQFVVYTALT IASEYLMLSY PMADFEGKSL
RPSIIISRIK KILPNLVEES SLYDLSKGND HFNKVISPIP TFNELIFALR RELEDEEIDE
EYWGEVYNWF KENEDFKWKI ENIFKGLRYS NTGEKVSRNK LLSLYKNDLG KLSFSVSRLE
KYAECPFSYF IQYGLKAKNR KVYEFTPPDL GSFVHDILDS FTNKVKKEKI AWSDLDMIKC
KNIVSELIDT KLKEDSGSIL NSTNKYKYFS KRFKRVISKS VSVISEQMRR GEFEVFNNEF
SFGSYNDGEA IVLELPSNEK VYLNGRIDRI DTLDLEGSTY LRIVDYKTGN KHFDLNEFYY
GLQMQLLVYL DALLKNSEYI LKKQALPGAV LYFRVDDPII KTKGDITTEE LEKEVLSNLK
MNGLILKDAK VVKAMDRGIE TDGYSLVIPA ALKKDGDFKA GSEVVTEEQF NLLREYVNKK
MIDLCEDMLC GDIKIQPTKD SDGSHCEFCD FSSICQFDSS IEDNKYKIIM KKSKDEIWNN
IRDELNDDKK EN
//
