ADDB_MOOTA
ID ADDB_MOOTA Reviewed; 1151 AA.
AC Q2RL78;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Moth_0481;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC18811.1; -; Genomic_DNA.
DR RefSeq; WP_011392018.1; NC_007644.1.
DR RefSeq; YP_429354.1; NC_007644.1.
DR AlphaFoldDB; Q2RL78; -.
DR SMR; Q2RL78; -.
DR STRING; 264732.Moth_0481; -.
DR PRIDE; Q2RL78; -.
DR EnsemblBacteria; ABC18811; ABC18811; Moth_0481.
DR KEGG; mta:Moth_0481; -.
DR PATRIC; fig|264732.11.peg.517; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
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; -; 4.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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.
FT CHAIN 1..1151
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379200"
FT DOMAIN 1..273
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 282..578
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 788
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1151 AA; 128371 MW; 0C219027507F504C CRC64;
MALRLVLGRA GSGKTRLCLE EIKAILAEGP AGPALIILTP EQATLQMELD LHRAAGVPGF
SRVQVLSFRR LGWRVFQEAG GAARPHLGEM GKAMALRAVV SAHRDDLGLF APLAGSPGFI
EQLAHTIAEL KLYRVTPADL DRILERYRET GREQTILARK LRDLALVYRE LETYLAGRYL
DPDDYLTLLA GRLPEAAFIR GARVWVDGFN GFTPQEEAVL QALMAVAEQV TVTLCLDPTL
RHRRLGETEL FHPTGETYHR LRQLALAAGV RVEDDVCLAG TPPRFREAPA LAHLEAHFGR
WPLRPFRGDA AGIRLVAAAN RRVEVEAAAR EILRLAREEN LSWRQMAVLV RDLEPYHDLI
VNTFRDFNIP LFIDRRRPVG HHPLVELVRA ALEAVLEDWA YDPVFRYLKS DLVPVPREEI
DLLENYVLAH GIRGRRWRDS RPWQYGNSRD LETPSPPGSA AGETINAIRE RASCHLRRFD
GALRGRQLTG REITAALFDL LQELGVPERL AAWSRQAAAA GDLDAAQEHE QIWEGLMDLL
EELVLALGDT SLELEEYAAI LDTGLESLKL RLIPPALDQV VAGTLDRSRQ PELQAAFVLG
VGEGVLPARL PEDATFSDRE REELRAAGLE LAPTGTLRLF HEEFLAYLAL TRSRRYLWLS
YPLADAEGKA LSPSPLVRRL RQLLPGLREE TAGTELPGGD DDLVYLTTPR QAAGHLARLL
GRGRPLPPLW QEVYRWLHQD ARGQKMLGLL EGGGYRNQVD PLEPELARGL YPRPLRLSIS
QLETFAGCPF RYFLSYGLGL QERRLYQVDP AGMGQFYHAA LKLFVEELGR RGLDWGRLSD
NEAAAIISQV VDSLAPALQH EILSSSARYG YLRKKLEQTL QRVMEVLNEH ARRGEFRPLA
VETSFGCRGK LPPLQLDAGP GRRVFLEGRV DRIDVARRQG RPYLRVIDYK SSPTTLDLTA
VYYGLALQLP LYLRAALDAA PELLGEAAEP AGMLYFAVRN PLIRQRGPVG KEAAARLRRQ
ELKMRGLLLD DVEVIKLMDR EIAASPDLLP LRLNKDGSLR KGAPVAGREE MALLLDLALA
RAAELAGAIL SGRVEISPYR RGQETACDFC PYRPVCAFDP QIPGSGYRRL GNLPGDFWQL
AAAFLGSQMK G
