ADDB_CLOBH
ID ADDB_CLOBH Reviewed; 1150 AA.
AC A5HYX0; A7G0V8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
GN OrderedLocusNames=CBO0426, CLC_0492;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
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; AM412317; CAL81979.1; -; Genomic_DNA.
DR EMBL; CP000727; ABS37895.1; -; Genomic_DNA.
DR RefSeq; YP_001252970.1; NC_009495.1.
DR RefSeq; YP_001386377.1; NC_009698.1.
DR AlphaFoldDB; A5HYX0; -.
DR SMR; A5HYX0; -.
DR KEGG; cbh:CLC_0492; -.
DR KEGG; cbo:CBO0426; -.
DR PATRIC; fig|413999.7.peg.430; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR PRO; PR:A5HYX0; -.
DR Proteomes; UP000001986; 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:0006310; P:DNA recombination; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..1150
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379172"
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"
FT CONFLICT 273
FT /note="N -> K (in Ref. 2; ABS37895)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="P -> L (in Ref. 2; ABS37895)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..442
FT /note="HKF -> YKS (in Ref. 2; ABS37895)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="A -> D (in Ref. 2; ABS37895)"
FT /evidence="ECO:0000305"
FT CONFLICT 1147
FT /note="Y -> C (in Ref. 2; ABS37895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1150 AA; 133523 MW; 978A27A358748C38 CRC64;
MSLRFIYGRA GSGKSQYCLN SIKNRIEEDI DRPLILLVPE QFSFQAEKNL IEVLDEKTGF
KTQVLSFKRM AYRVFNEVGG ITAKHMNESG KSMLLYNIIE DNKNNLKVFK KAAKRQGFIT
TISDIITEFK RYNITPEIIL NNLENIEGDN LKYKMEDLAL IFSQFETRLH KNYIDNEDDL
TILAEKLNKS KQFDNAEIWI DEFSSFSPQE YSVLEKLLLK SYRINITLCT DYLNQGRFVD
TTDVFSPIKN TENKLLQIIE DNNIKLDKPI ALNCDPCARF KNSAELQHLE KNMFSFPYKE
YKNETKDICM LKTLNQFTEI ENTAKDIIKL CIDKGCRFKD IAVITGDLEG YENIISSVFL
QYNIPFFIDK KREINNNPII VLILSALEVL SKNWTYESVF RYLKTGLLDI NNEEMDILEN
YVLANGIKGY QWTNDKPWEH KFFSNYELED QVEKELLAKI NDIRYKAMEP IVTLNKNFKS
IDKAKEFCEV LYEFLCNINL PDKIQNMIED FKVEGEIEKA SEYNQIWNIV MEVLDQIVEV
IGEEKISLKE FFKILQTGLS EYEIGLIPPT LDQVMVGSIT RLRSHNINTL YIVGVNDGIF
PSPLKEEGIL SDDDRKFLGD KGLEIAKDTK SIAFEEQFLV YSTLTTPSKY LRLSYPIADG
EGKTLRPSII ISRIKKIFTN ICEENDIVKL NGEEEELKNI SSAKPTFNYL ISNLRKDVEG
AKIDNIWGDT YKWYLENEFW IEKLNRLIKG FDYTNQSKYI ETKKIRNLYG KPLKISVSRV
EKFSQCPFAY FVQYGLKAKD RKIFNLSYPD LGIFMHSILE KFSHELEKQG LEWDTMDLNW
AEEEIDKLIN EELDNKSLDI LNSSKRYEYV TKSVKKILKR SIWLIGEHIK RGNFKPSYYE
LSFDIDGDYP PIAMELHSGE VVNLIGRVDR VDLLQKDGAT YLKIIDYKSG AKEFKLSDVY
YGLQLQLLIY LDAILTELAE RSGINGEPGA LLYLKLDDPI VKNTVDMSDE EIEKSIIKNL
KMKGLILNDP NVIRDMDNII SGISDIIPVM VKKDGGVSEG RSSVATKEEF ETLRKYVRYT
IIEICEEMLE GNIEIKPYKK KDGSSCDYCI YSSVCKFDTN IRGNKYNILI DKKDEEVWDA
IKKKLEYKNI
