ADDA_MOOTA
ID ADDA_MOOTA Reviewed; 1405 AA.
AC Q2RL77;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Moth_0482;
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 AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000255|HAMAP-Rule:MF_01451}.
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_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; CP000232; ABC18812.1; -; Genomic_DNA.
DR RefSeq; WP_011392019.1; NC_007644.1.
DR RefSeq; YP_429355.1; NC_007644.1.
DR AlphaFoldDB; Q2RL77; -.
DR SMR; Q2RL77; -.
DR STRING; 264732.Moth_0482; -.
DR PRIDE; Q2RL77; -.
DR EnsemblBacteria; ABC18812; ABC18812; Moth_0482.
DR KEGG; mta:Moth_0482; -.
DR PATRIC; fig|264732.11.peg.518; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; MEHYALR; -.
DR GO; GO:0008408; F:3'-5' 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-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
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_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
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 InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 3.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 3.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 2.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1..1405
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379301"
FT DOMAIN 7..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 551..914
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1405 AA; 153610 MW; 3EF670FF2CB95D50 CRC64;
MTATGKREWT PDQLAAIRAR RANILVAAAA GAGKTAVLVE RIIQRLTDPE DPVSLENLLV
VTFTEAAAAE MRQRIGAALE AAVARDPENE ALRRQLLLLN RAHISTIHSF CLWVLRTYFY
RLDLDPGFRV MDPAEVDLMQ LEVMDRVLEE AFAAEPDGGP VTDLADSLGG RGDANLVDLV
LRVWEFSRSL PWPEAWLEQV TSSYKVTPET PLESLPWYGE LRQMITLELQ EAAWYLEQAR
QAAAAPGGPA VYLDNLENEK EQVTRLLEEV GDLPWEELNA KLAAVHFGRL KAARGEDVDP
VLKERAGKLR NQARDLLYAL KEDLCRDEAA VRAELERSGE LVATLVGLVR RFDAALREAK
GRRNLIDFSD LEHLCLRVLL DEGAGPGRLQ PSDVALELRQ RFAEVLVDEY QDINTVQDAI
LALVSRQDVA ENNLFMVGDV KQSIYRFRLA NPDLFLAKYR QYPEGEGGPN RRILLKANFR
SRQGVVDGVN FIFRQVFSPL VGELEYDAAA ALVGRAGYPE NPAAATPAVE VYLQEGKVAA
GTGAGGRTDL PEAVGAGKGG KISGGAGYGE TLSGYGAASP GGETGAPDLE DLTALEREAL
LVARRIRRMV RGTPERPGPE FQVWDQEKKE YRDLTYRDIV ILLRATRDRA PVFLEALKQY
GIPAYADLGS GYFAATEIET ILSLLRVIDN PHQDIPLAAV LRSPIVGLSA GDLARIRLAA
PGEDFFTAVV KAAGAPLLPF TARESAAPSS TATGSGGALD NQPGQDPVCI APYIEDTQEP
WRDDHPGPGA AAGKAVPGKD RDLASLLREF LARLERWRTL ARRQPLGDVI WQLYRETGYL
EFVGGLPGGA QRQANLRALL DRARQFEGFA RHGLFRFLRF IERLQQNEGD LGTARALGEN
EDVVRVMSIH RAKGLEFPVV IVAGLGKGFN LRDLSGDFLL HGRLGLVPLY LDAAAGIKYP
TLPYLATGHR LRLEALSEEL RILYVALTRA REKLILAGTV RDLPRQAENW CASLFLPGEQ
LPPVLTSRAG NPLDWLLPAL ARHPDAAAIR DLAGVGGGHL LPDPSSWQVE VVRGGELPDR
GSEEPGVQVR VTAGYQGTES AGQQENPGLL CSGWPGGSRE LAGAVTPVQE TAGKTVAPPG
SNIAEAGVEP GVSPPAGAVS PQDETGPTWL QQEVARRLAW TYPRQPLTAL PVKLTVTDLK
RRFDVFNEGE TPLRPGENTF TRRPAFLQSH QGLTAAERGT ATHLVLQHVD LSRPVTGESL
AGLLQEMVER EILTPEQAAA VDIRAIVTFF AAPLGKRLLA RWEQVKRELP FSLAVPAVEL
YPGLPAEAAA GEIILVQGII DCLVEEEDGF LLLDFKTGRI PPDPLAAYRE QVRFYTRAVE
TIFNRNVKEV HLYFLDGGVD FKVTS
