ID   ADDA_CLOP1              Reviewed;        1271 AA.
AC   Q0TV46;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=CPF_0025;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   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; CP000246; ABG82931.1; -; Genomic_DNA.
DR   RefSeq; WP_011590031.1; NC_008261.1.
DR   AlphaFoldDB; Q0TV46; -.
DR   SMR; Q0TV46; -.
DR   STRING; 195103.CPF_0025; -.
DR   PRIDE; Q0TV46; -.
DR   EnsemblBacteria; ABG82931; ABG82931; CPF_0025.
DR   GeneID; 29569845; -.
DR   KEGG; cpf:CPF_0025; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001823; 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..1271
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379262"
FT   DOMAIN          3..476
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          528..824
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   1271 AA;  147384 MW;  20E380EBC01A3540 CRC64;
     MGTKWTEEQE LAINTRKCNL LVAAAAGSGK TAVLVERIIK MITEGENPVD IDKLLVVTFT
     NAAASEMRER IGDAISKALE KDPSSEALQR QLALLNRASI TTMHSFCLEV IKNNFHLIDL
     DPGFRIGDQT ECELIKQDIL ADLFEDMYAK DDECFKDLVE AYGGSKSDDN LNSIILKFYN
     FIMSGPWPET WLKDKVEEFN INSIEELEGK KWIEVLKESI ILDLNNAYSM LTQARDIAEM
     GGGLEPYLVN IYPEIIQVEE LRIALSEGIV KFYNKLMGAS FGRLKSVRKA SVDDERALEK
     AKSLRDESKK IIENLRDNVF ETSLEEAVLG MKKMYPLMKC LSGLVIEFSN RYRDKKREKD
     ILDFNDLEHL CLEILIDKDE EGNIKPSQVA LEFKDKFEEV LVDEYQDSNT IQETIVGMVS
     RRDVENPNVF MVGDVKQSIY KFRQANPELF LEKYINYREF EDSNRKIMLY KNFRSREEII
     NGVNYIFKTL MSNTVGELEY DEKEALNLGA SYGELNEENV EKEYIDEIEN LKVAGDIELN
     ILNKAGNKEY RDDDELGEEE EDLDSIQLEA RIIGKKIKEL MNPEDGSHYM VFDKDLGKYR
     RIKYKDIVIL LRATKNWAET FVDELGTYGI PVYADTGTGY FQTIEIRTIL ALLHIIDNPM
     QDIYILSALR SPIFSFTSEE FADLRLLNKD KYFFEIIKEV VDGIYDESIS KELKGKCKYF
     LDYLNKWREK AAYMPIDEFI WFLYSDTSYY GYVGTMPNGV QRQANLRILF QRAKQYESTS
     FKGLFNFINF INKLKKSSGD MGSAKILGEN ENVVRIMSIH KSKGLEFPVV ILGGTGKQFN
     KMDLREDILL HETLGIGTNC IDVKKRIKYD TLQKHAIKKK CELEVLSEEM RILYVAFTRA
     KEKLIITGAV SDLEKSCENW CKASASSGDN RINPGNVLKG KSYLDWICMA LTKHKDGDAI
     RNIGNGDITL NLDDKSNWSF KSWDRSELLE TNNNKKEKNN IDIFESNNWI ESKKDIKEVI
     EIRDRLGFKY KYIESCNTPS NISVTELKRA HQEEEFMQES YNIIDNESNE ENKKEKIKRK
     PRFMEERQEE FSAAKKGTIT HFVMQHIDLD KVTYIDEIRE EVLKMVKKEL LTEEEGKVVN
     VFKIQKFFKS DLGQRMLNSY KSGKKVYREL PFITEIPSSI IEKNLDPKIY GEEKVRLQGI
     IDAFFEEEDG YVLLDYKTDY VKEGEEEDFI NKYKIQINLY KDTLNKILGE EVKEAYLYSF
     YLEKELKISK E