ADDB_ACET2
ID ADDB_ACET2 Reviewed; 1146 AA.
AC A3DH20;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Cthe_2040;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) 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 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; CP000568; ABN53249.1; -; Genomic_DNA.
DR RefSeq; WP_003514090.1; NC_009012.1.
DR AlphaFoldDB; A3DH20; -.
DR SMR; A3DH20; -.
DR STRING; 203119.Cthe_2040; -.
DR EnsemblBacteria; ABN53249; ABN53249; Cthe_2040.
DR KEGG; cth:Cthe_2040; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000002145; 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; IPR014017; DNA_helicase_UvrD-like_C.
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.
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; Exonuclease; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1146
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379185"
FT DOMAIN 1..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 276..584
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 786
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1105
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 1114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1146 AA; 130446 MW; 34D860C208308F0D CRC64;
MSLRFIYGRA GSGKTRFCLE EIKSRITSKA THPLVLLVPE QFTFQAERDL ISVLGTGGIL
KTEVLSFSRI AYRTFNEAGG ITYPHIHSAG KCMILYRILD KMKGSFRVFS KTADRQGFVN
TLSTLITEFK KYNVTPEDLE KVSKELEEDN PVKEKLMELT AIYDLFEKTI AERYRDPDDD
LTLAAKKLGS IPLYDGAEIW IDGFTGFTPQ EYQIIGQLMK KAQRVNISFC TDCLDGDLND
TDIFSSIKTA YRKLVKMAKE NGIPVEPSVV LNSKPLFRFS QSPELSHLEQ YLYAYPYKTY
NEKTKDISLF SSVNIFAEVE ACARDIVRLC RDRGMRYREI AVVTGNLDGY EKLIEAVFSE
YGIPCFIDRK VDIVNHPLVR LIMSMLDIFI ENWSYEAVFR YLKTGLTGID RESIDRLENY
VLACGIRGSC WTETEEWKMV PELIPNEKSL EEAKELLEDV NRIRAQVVAP LMEFRKKTKG
RKKASDFCAS LYDFLCTLGI PEKIEDAIEK FRESGNLNLA NEYSQVWNAV MEVFDHTVEV
MGDETFGIEK FARILEIGFG ECKIGLIPAS LDQVLVGSLE RSRSHEIKAL YILGANDGVF
PPAVMEEGIL SDQDRAVLNN AGIELASDTR TQAFDGQYLI YRALTTAGNY LRISWSIADH
EGRTLRPSLV VFRLRKLFLN ITETSNILPS GSLEEEMELL SGNSPAFKSM VSALRQKADG
KEIKPVWQEA YRWFAVQDEW RGKCEALRAA FQYKNLAQPV SREKIAALYG EPAVSSVSRL
EKYTACPFAF YVQYGLGAKE RQIYSLRPPD VGTFMHAVIE KFSRMVAKRN ISWRDLDRDW
CSEKVSEIVD EMLEKMQGSG IAASRRYTAL TLRLKRVVAR AVWLIAEHIR RSSFEPVAYE
VGFGENGKYP PIVIELDSGE KIHLTGRIDR VDALKTEDGT YLRIVDYKSG GKDFKLSDVF
YGLQIQLITY LDALWESGEA DENNPVLPGG VLYFKIDDPI IRGNGRMTEE EIEKAIMKQL
RMKGLLLADV KLIREMDKDI EGSSMIIPAT VNKDGSLGKN TSAATMEQFK LLRKYVRKLL
KNLCEEIMKG NVSINPYKKK GTTSCKYCSF LPVCQFDTTM KENTFKLLYD KKDDEIWSLM
AQEEEE
