ADDA_CLOAB
ID ADDA_CLOAB Reviewed; 1252 AA.
AC Q97GV3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=CA_C2262;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80219.1; -; Genomic_DNA.
DR PIR; H97178; H97178.
DR RefSeq; NP_348879.1; NC_003030.1.
DR RefSeq; WP_010965560.1; NC_003030.1.
DR AlphaFoldDB; Q97GV3; -.
DR SMR; Q97GV3; -.
DR STRING; 272562.CA_C2262; -.
DR DNASU; 1118445; -.
DR EnsemblBacteria; AAK80219; AAK80219; CA_C2262.
DR GeneID; 44998740; -.
DR KEGG; cac:CA_C2262; -.
DR PATRIC; fig|272562.8.peg.2462; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000814; Chromosome.
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; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 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; Reference proteome.
FT CHAIN 1..1252
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379247"
FT DOMAIN 6..489
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 523..811
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1252 AA; 145509 MW; B161178C0AA60F7D CRC64;
MNVGKTNWTE EQKEAIDTRN CNLLVAAAAG SGKTAVLVER IVKIITNEEN PVDIDRLLVV
TFTNAAASEM RERIGDAIVN KLCENPNSRV IQKQLALIGK SKITTIHSFC LDVIKNNFHM
LDLDPDFRVG DETEIILLKN ETLEELFEDK YLQAEYTSKG INKNNNSIEF LKLVESYCGN
KNDQVLFNMV MNLYNFSMSN PEPYKWLKKA AERFNVDDDF EFGDSLWAEV LMKNIQIQLL
GMKGQLIESI NIINSCASIE SYRENLEVEL SMLEKLIVAS NNYEKLYEEL KNVQFKTLKR
CPKDADKEKQ KLVRDLRDGV KKSLSKISED ILSQNSEEIK EEFKVLYPLM KTLSELVIEF
DIRYKDKKKK RGIIDFNDFE HMCLSILTKS DESGNIVPSE TALKIREKYE EILIDEYQDS
NMVQEVILST ISRKDTENPN LFMVGDVKQS IYRFRQANPG IFLEKYNSYK ENKDEKNRKV
LLYKNFRSRK EVLDSVNFVF KQIMSVNIGE LDYDDNEKLN LGANYEEIEE NLISHSAELN
IIEKSEDNTE IKENNEDEES VDNIMLEARL IGRRIIELKE NFKVLDKNTN VYRKAEFKDI
VILLRSTKGW ANVFSDELKN MGIPVFADAN SGYFDAPEVK TMLSLLQVID NPRQDIPMAA
VLKSPVGGFS VEDLIDIKVI EGDTFYDKLK VAADIGDDEF SVRIRTFLNR LYRWRKESLY
TPIDEFIWYL YTDTGYYGYV GAVSGGIQRQ ANLKMLFQRA KIYSETSYKG LFNFINFINK
LKLTSGDMGS AKILGENENV VRIMSIHKSK GLEFPIVFVG GLGKNFNLMD MNNPVLFHNY
LGFGPEYVDY KKRISHKTLA KEAIKNRIRI ETLSEEMRIL YVAFTRAKEK LIMVGSVSDI
KRSVFKWAVN LRSNQNKISE DYVLKSKSFL DWIASAVIRH KDAENLRDIM DTSKENIDNL
VCDPSSWRVN VLSRNDVLSF NQLLLEEEKN INEKLTQFYK RLKEIRSSNY ESVYIEEIKS
RLEFKYRYEK AAELPSLLSV TELKRNINED NDEYATKIFT PSLVKKPLFL EEVKKMSPSE
RGTAVHSVMQ HLDFSSISCD MSIKNIRHQI DDMVFRRILT EKQAESVNIN RILKFFQSPI
GSRVIKAEKV YREFPFQIRV KSTEIYNDLP KIYDDENIIV QGIVDLFFKE NDEIVLLDYK
NDYINDENLN ETVKKYTYQI NYYKRALEIV TGLKVKEKYL YLFYTGDTIK IE
