ADDB_CLOBK
ID ADDB_CLOBK Reviewed; 1150 AA.
AC B1IEL7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CLD_0317;
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1;
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; CP000939; ACA44815.1; -; Genomic_DNA.
DR RefSeq; WP_003399595.1; NC_010516.1.
DR AlphaFoldDB; B1IEL7; -.
DR SMR; B1IEL7; -.
DR PRIDE; B1IEL7; -.
DR EnsemblBacteria; ACA44815; ACA44815; CLD_0317.
DR KEGG; cbb:CLD_0317; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000008541; 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..1150
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379175"
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 1150 AA; 133493 MW; 23B85ADB8AAE6F23 CRC64;
MSLRFIYGRA GSGKSQYCLN SIKNRIEEDI DRPLILLVPE QFSFQAEKNL IEVLDEKTGF
KTQVLSFKRM AYRVFNEVGG ITAKHMNESG KSMLLYNIIE DNKNNLKVFK KAAKRQGFIT
TISDIITEFK RYNITPEIIL NNLENIEGDN LKYKMEDLAL IFSQFETRLH KNYIDNEDDL
TILVEKLNKS KQFDNAEIWI DEFSSFSPQE YSVLEKLLLK SYRINITLCT DYLNQGRFVD
TTDVFSPIKN TENKLLQIIE DNNIKLDKPI ALKCDPCARF KNSAELQHLE KNMFSFPYKE
YKNETKDICM LKTLNQFTEI ENTAKDIIKL CIDKGCRFKD IAVITGDLEG YENIISSVFL
QYNIPFFIDK KREINNNPII VLILSALEVL SKNWTYESVF RYLKTGLLDI NNEEMDILEN
YVLANGIKGY QWTNDKPWEH KSFSNYELED QALKELLAKI NDIRYKAMEP IVTLNKNFKS
IDKAKEFCEV LYEFLCNINL PDKIQNMIED FKVEGEIEKA SEYNQIWNIV MEVLDQIVEV
IGEEKISLKE FFKILQTGFS EYEIGLIPPT LDQVMVGSIT RLRSHNINTL YIVGVNDGIF
PSPLKEEGIL SDDDREFLGD KGLEIAKDTK SIAFEEQFLV YSTLTTPSKY LRLSYPIADG
EGKTLRPSII ISRIKKIFAN ICEENDIVKL NGEEEELKNI SSAKPTFNYL ISNLRKDVEG
VKIDNIWGDT YKWYLENEFW IEKLNRLIKG FDYTNQSKYI ETKKIRNLYG KPLKISVSRV
EKFSQCPFAY FVQYGLKAKD RKIFNLSYPD LGIFMHSILE KFSHELEKKG LEWGTMDLNW
AEEEIDKLIN EELDNKSLDI LNSSKRYEYV TKSVKKILKR SIWLIGEHIK RGNFKPSYYE
LSFDIDGDYP PIAMELHSGE VINLIGRVDR VDLLQKDGAT YLKIIDYKSG IKEFKLSDVY
YGLQLQLLIY LDAILTELAE RSGINGEPGA LLYLKLDDPI VKNTVDMSDE EIEKSIIKNL
KMKGLILNDP NVIRDMDNII SGISDIIPVM VKKDGGVSEG RSSVATKEEF ETLRKYVRYT
IIEICEEMLE GNIEIKPYKK KDGSSCDYCI YSSVCKFDTN IRGNKYNILI DKKDEEVWDA
IKKKLEYKNI
