ADDB_CLOTE
ID ADDB_CLOTE Reviewed; 1150 AA.
AC Q897P5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=CTC_00686;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO35291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015927; AAO35291.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_035124448.1; NC_004557.1.
DR AlphaFoldDB; Q897P5; -.
DR SMR; Q897P5; -.
DR STRING; 212717.CTC_00686; -.
DR PRIDE; Q897P5; -.
DR EnsemblBacteria; AAO35291; AAO35291; CTC_00686.
DR KEGG; ctc:CTC_00686; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001412; 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; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 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_0000379184"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 789
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1150 AA; 134317 MW; 7EB3E9AABFEFF91E CRC64;
MSLKFIYGRS GSGKSYYCFQ DIKRKIEENS DKKLILLVPE QFSFQSEKNL INYIGERAVS
RAEVLSFKRM AYRVFNEVGG VTHRYMNESG KNMLLYSILN ELTGELKIFN NAANKNGFVS
TLSDIITEFK RYNLTPEMIK EYLEVAEERE DNILKGKLQD IYLIYSKFQD SIRKKFIDEE
ENLTILADKL KESKYFDGAY IWVDEFFNFT PQEYLVLEEL LLKAEKVNIT LCTGGLNEGE
RIDNLDLFLP VKNTEEKILE FVKRNNIKYE KPIKLNCDPC YRFKNSKELS HMEKNLFAFP
YKIHEKYTED ICVFQALNEY SEIEYTARDI IKLVRDNGFR YKDIAVITGD LEGYQSLIKA
VFTEYGIPYF IDKKVEGDNN PLVIFILSSL EVLNKNWNYE SVFRYLKAGL VDIKREEIDI
IENYVLANGI RGKRWIEEKD WDYKILYGFN LTEEKEEEEE EKLKKINEIR RKITEPLIEF
HNNIKGEITP KKMCLELYNF LEKMNISSKI ESWIKYFKER NRLDKINEYK QIWDVAIGLM
EQLVEVMKEE KLNSRTLENI FKSGFEQYEL GIIPPSLDQV LVSSTKRLRS HEIKALYIVG
TNDGVFPSVL DENGILSDLE RENLRETGLE VAKDTKSTAF EEQFLMYVTL TTMSDYLRIS
YPIANEEGKT LRPSIVISRL RKIFPNLCEK SNVIKEEGDI EKISSPKPTF NEFISQLRVK
EEGLELSSIW LSVYDWFMNN KEWKEKFINI SQGFNHTNYA EIVDTRRVRK LYGSKLNMSV
SRLEKFSQCP FAYFIRYGMN AKERKIYKVS TPDIGTLMHD VVESFSRHIE GKNISWEEID
RELCESFVST MVDEKIKDMK GSILNSSPRY KHMTNRIKDI LSKSMEVISQ QISRGDFKPS
AYELAFGFNG DFPPISIELS SGEKVNLIGR IDRVDKLENE DGTFIRIIDY KSGKQDFNLS
DIYYGLQIQL LVYLDALLQE IEDSAKKEVN PAGILYFNMD DPLISTKKEI TKEEAEKEIL
KKLKLKGLVL KDANIIKAMD NLISGYSDII SVRVNKDGSP SKNSSVADLE DFQLLRDYVR
KLIVELCEEM LEGNISIKPY KKNNYTPCGF CDYSAICQFD TSIKGSQYRF INDKKDDEVL
QCIREEMKED
