ADDB_THEP3
ID ADDB_THEP3 Reviewed; 1149 AA.
AC B0KDB8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Teth39_2011;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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; CP000924; ABY95637.1; -; Genomic_DNA.
DR RefSeq; WP_009051917.1; NC_010321.1.
DR AlphaFoldDB; B0KDB8; -.
DR SMR; B0KDB8; -.
DR STRING; 340099.Teth39_2011; -.
DR EnsemblBacteria; ABY95637; ABY95637; Teth39_2011.
DR KEGG; tpd:Teth39_2011; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000002156; 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 PANTHER; PTHR11070; PTHR11070; 1.
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..1149
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379224"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 784
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1102
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 1111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1149 AA; 134381 MW; 96CE99595D768C71 CRC64;
MGIRFIYGRA GTGKTYFCLR EIKEKINDGN SHPLILLVPE QFTFEAEKYL LETVEKDRKM
RAQVLSFKTL ANRVFTEVGG LTRQHVNSCG RSMVIYKIME DLKENLKVYY KASRQQGFIK
KISEVITEFK RFEVTPEKLM DTAESIQKEG LREKLRELSL IYGKFDELLH QKYIDEEDAL
TLLAEKLEYS EQFKGAEFWI DGFTGFTPKQ YKVLEKLLKK AARVSVTLTM DTSKDSIDNT
DLFYTTKKTE DKLLKICYEN NISYEKPVDL NEGVPKRFEK NEEMAFLEKH LFSYPYKIYS
KDTKNISLFK AVNVYSEVEE TAREIIRLVR DENLRYSDIV VTARDLKRYH KLIKTIFSHY
GIPHFIDLKL DIKNNPIIVY ITSLFEIYLK NWSYESVFRH LKTGFTNLNK EDISFLENYV
LANGIKGGKW KEEWKYSFRN RLDKLFDDQD EKEALEKVNT IKNGISEPLN KFYKDFSNAN
TVREACEILY NFLVERDIPQ RIENLIREFK ENKEFEIANQ YSQIWDIVVD VLDQMVEVMG
EEKINIDLFS KILDIGFEAY QIGSIPPALD EVLVTSVDRM KSHNAKALFV IGANDGIFPA
SSFEEGILTD EDRQILTSYE VELDRDTKAK VFEEQFLVYT ALTSTSKFLR ISYPIADHEG
RSLRPSIIIS RFKRIFPQIT QFSNVIEMDT DEENLHRVSS PDPTFNEMIK SFKEWDIKDK
INSLWLDVYN WYSNKEVWRK RIEKVLEGFN YSNQVRVIPS AKIKRLYKDE INFSVSRLEK
YAACPFAYFV QYGLKAKERK IYSFDPPDLG IFMHNVLNEV SKALEKEDKT WEDLDREYCD
EVVNIVVDNM LKGVSEHILK SSPRYEYLSK RLTRVLSNAV WVISEHIKRS SFIPSGHEVA
FGENQMYPPI KIILSNGEEI NLIGRIDRVD VFEKGEESYI RIIDYKSGNK ELKLEDVFYG
LELQLLIYLD AILESADKEN TDIKPAGIFY FRIDDPIVKA DKDITDEELQ KEILKKLRLD
GLVLKDAEII KEMDKSINGT SYIIPASINK DGTIGKKTKG ATKEQFELLR KHVKNMIKDL
AEQMINGNIS ITPYRKGKET ACKYCPYSSV CKFETNFEGN KYMFIKEQKE EEIWNMLQKE
VNKDGDKVD
