ADDB_CLOBM
ID ADDB_CLOBM Reviewed; 1147 AA.
AC B1KUY8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, 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 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=CLK_3628;
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA55502.1; -; Genomic_DNA.
DR RefSeq; WP_012343473.1; NC_010520.1.
DR AlphaFoldDB; B1KUY8; -.
DR SMR; B1KUY8; -.
DR PRIDE; B1KUY8; -.
DR EnsemblBacteria; ACA55502; ACA55502; CLK_3628.
DR KEGG; cbl:CLK_3628; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000000722; 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; -; 3.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02773; addB_Gpos; 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..1147
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379174"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 786
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 1147 AA; 133345 MW; ABEEEBE0F7D69D32 CRC64;
MSLRFIYGRA GSGKSQYCLN SIKKRIEEDI DRPLILLVPE QFSFQAEKNL IEVLDEKTGF
KTQVLSFKRM AYRVFNEVGG ITAKHMNESG KSMLLYNIIE DNKNNLKVFK KAAKRQGFIT
TISDIITEFK RYNITPEIIL NNLENIEEDN LKYKMEDLAL IFSQFETRLH KNYIDNEDDL
TILVEKLNKS KQFDNAEIWI DEFSSFSPQE YSVLEKLLLK SYRINITLCT DYLNQGRFVD
TTDVFSPIKN TENKLLQIIE DNNIKLDKPI ALNCDPCARF KNSIELQHLE KNMFSFPYKE
YKNETKDICM LKTLNQFTEI ENTAKDIIKL CRDKGCRFKD IAVITGDLEG YENIISSVFL
QYNIPFFIDK KREINNNPII VLILSALEVL SKNWTYESVF RYLKTGLLDI NNEEMDILEN
YVLANGIKGY QWTNDKPWEH KSFSNYELED QVEKELLAKI NDIRYKAMEP IISLNKNLKN
KERAKEFCEV LYEFLCSINL PDKIQNMIED FRAEGEVEKA SEYNQIWNIV MEVLDQIVEA
IGGEKISLKE FFKILQTGFS EYEIGLIPPT LDQVIVGSIT RLRSHNINIL YIVGVNDGIF
PAPLKEEGIL SDDDRQFLGD KGLEIAKDTK SIAFEEQFLV YSTLTTPSKY LRLSYPIADG
EGKTLRPSII ISRIKKIFTN ICEENDIVKL NGEEEELKNI SSAKPTFNYL ISNLRKDIEG
VKIDNIWGDI YKWYFENEFW IEKLNRLVKG FDYTNQSKYI ETKKIRNLYG KPLKISVSRV
EKFSQCPFAY FVQYGLKAKD RKIFNLSYPD LGIFMHSILE KFSHELEKKG IDWDTMDLNW
AEEEIDKLIN EELDNKSLDI LNSSKRYEYV TKSVKKILKR SIWLIGEHIK RGNFKPSYYE
LSFDIDGDYP PIAMELHSGE VVNLIGRVDR VDLLQKDGAT YLKIIDYKSG TKEFKLSDVY
YGLQLQLLIY LDAILTELAE RFGIDGEPGA LLYLKLDDPI VKNIVDMSDK EIEKSIIKNL
KMKGLILNDP NIIKDMDNII SGISDIIPVM VKKDGGVSEG RSSVATKEEF ETLRKYVRYT
IIEICEEMLE GNIEIKPYKK KDGSSCDYCI YSSVCKFDTE IRGNKYNILI DKKDEEVWEA
IKKKLEC
