ID   ADDA_CLOPS              Reviewed;        1270 AA.
AC   Q0SWW4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=CPR_0025;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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; CP000312; ABG86634.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SWW4; -.
DR   SMR; Q0SWW4; -.
DR   PRIDE; Q0SWW4; -.
DR   EnsemblBacteria; ABG86634; ABG86634; CPR_0025.
DR   KEGG; cpr:CPR_0025; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001824; 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.
FT   CHAIN           1..1270
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379263"
FT   DOMAIN          3..476
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          528..823
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1270 AA;  147050 MW;  D296A501E20DA8F9 CRC64;
     MGTKWTEEQE LAINTRKCNL LVAAAAGSGK TAVLVERIIK MITEGENPVD IDKLLVVTFT
     NAAASEMRER IGDAISKALE KDPSSEVLQR QLALLNRASI TTMHSFCLEV IKNNFHLIDL
     DPGFRIGDQT ECELIKQDIL ADLFEDMYAK DDECFKDLVE AYGGSKSDDN LNSIILKFYN
     FIMSGPWPES WLKDKVEEFN INSIEELEGK KWIEVLKESI ILDLNNAYSM LTQARDIAEM
     GGGLEPYLVN IYPEIIQVEE LRIALSEGIV KFYNKLMGAS FGRLKSVRKA SVDDEKALEK
     TKSLRDESKK IIENLRDNVF ETSLEEAVLG MKKMYPLMKC LSGLIIEFSN RYRDKKREKD
     ILDFNDLEHL CLEILIDKDE EGNIKPSQVA LEFKDKFEEV LVDEYQDSNT IQETIVGMVS
     RRDVENPNVF MVGDVKQSIY KFRQANPELF LEKYINYREF EDSNRKIMLY KNFRSREEII
     NGVNYIFKTL MSNTVGELEY DEKEALNLGA SYGELNEENV EKEYIDEIEN LKVAGDIELN
     ILNKAGNKDY SDDELGEEEE DLDSIQLEAR IIGKKINELM NPEDGSHYMV FDKDLGKYRK
     IKYKDIVILL RATKNWADTF VDELGTYGIP VYADTGTGYF QTIEIRTILA LLHIIDNPMQ
     DIYILSSLRS PIFSFTSEEF ADLRLLNKDK YFFEIIKEVV DGIYDESISK DLKGKCKYFL
     DYLNKWREKA AYMPIDEFIW FLYSDTSYYG YVGTMPNGVQ RQANLRILFQ RAKQYESTSF
     KGLFNFINFI NKLKKSSGDM GSAKILGENE NVVRIMSIHK SKGLEFPVVI LGGTGKQFNK
     MDLREDILLH ETLGIGTNCI DVKKRIKYDT LQKHAIKKKC ELEVLSEEMR ILYVAFTRAK
     EKLIITGAVS DLEKSCENWC KASASSEDNR INPGNVLKGK SYLDWIGMAL TKHKDGDAIR
     NVGNGDITLN LDDKSNWSFK SFDRSELLET NNNKKEKNNI DIFESNNWIE SKKDIKEVIE
     IRNRLGFKYK YIESCNTPSN ISVTELKRAH QEEEFMQESY NIIDNESSEE NKKEKIKRKP
     RFMEERQEEF SAAKKGTITH FVMQHIDLDK VTYIDEIREE VLKMVKKELL TEEEGKVVNV
     FKIQKFFKSE LGQRMLSSYK SGKKVYRELP FITEIPSSII EKNLDPKIYG EEKVRLQGII
     DAFFEEEDGY VLLDYKTDYV KEGEEEAFIN KYKIQINLYK DTLNKILGEE VKEAYLYSFY
     LEKELKISKE