ID   ADDA_CLOD6              Reviewed;        1275 AA.
AC   Q18AN9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=CD630_10410;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ67882.1; -; Genomic_DNA.
DR   RefSeq; WP_011861079.1; NZ_CP010905.2.
DR   RefSeq; YP_001087522.1; NC_009089.1.
DR   AlphaFoldDB; Q18AN9; -.
DR   SMR; Q18AN9; -.
DR   STRING; 272563.CD630_10410; -.
DR   PRIDE; Q18AN9; -.
DR   DNASU; 4914431; -.
DR   EnsemblBacteria; CAJ67882; CAJ67882; CD630_10410.
DR   KEGG; cdf:CD630_10410; -.
DR   KEGG; pdc:CDIF630_01181; -.
DR   PATRIC; fig|272563.120.peg.1081; -.
DR   eggNOG; COG1074; Bacteria.
DR   OMA; KQSIYRW; -.
DR   PhylomeDB; Q18AN9; -.
DR   BioCyc; PDIF272563:G12WB-1160-MON; -.
DR   Proteomes; UP000001978; 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..1275
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379257"
FT   DOMAIN          4..481
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          531..839
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         25..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1275 AA;  147378 MW;  16F8EAED257697ED CRC64;
     MSSPKWTKEQ LEVIESRECN LLVAAAAGSG KTAVLVERII QMITSRENPI DIDKLLVVTF
     TNAAASEMRE RIGDAIGKAL DENPENKHLQ NQLVLLNKSS ITTIHSFCLD VIKSNFHRIN
     LDPNFRIGDQ TECAILKQEA IEEVFEDLYE ERDEGFLNLV ESYAERGGDK EVQDIILGIY
     SFAMASPEPK KWLIDSAERF NIDENFDFSQ SIWARAILDT VKIEINGLCL NMERALKEVE
     SIEELETFAE KLSVEYKKIA DISQACNKSW DEAYKKMASM SFENYVKGVK RISKDAPSYI
     KESKEKAKTI RDKTKKSLES IVSATFNKDN DSIREEIKYL YNIVKPISSV VLRFEEEYSN
     KKREKGIIDF NDIEHFALNI LTDVDEKGNI VPSDIAVGYR NKFYEIFIDE YQDSNLVQEV
     LLKAVANTET PNRFMVGDVK QSIYRFRQAK PELFLQKYNN YNDKKGSSHR KIMLYKNFRS
     REEVVDAVNY IFENIMNENI GEIEYTEKER LNLGANFNVD TDEKSIIGGA TEIHLIQKDN
     KLDDDIINDK DDRINNKENE IEEEEKLDNI QLEARMVGNI IKDLMKVNED GKIQKVYDKG
     IDGYRPVEFR DIVILLRATS AWAPVFADEL MNMDIPTYAD VGVGYFDTIE IKTILSLLQI
     IDNPMQDIPL ISVLKSPIFG FTPEDLIDIR VQSKDKIFYE VLKSTAEYDG FTDSQNENES
     EFIPSEECIN KSKDFLIKLK EFKEKSMYMS TDEFIWYLYT RTGYYAYVGA LPGGSQRQAN
     LKVLFERAKQ FEETSLKGIF NFVNFIEKLK KSSSDMGSAK TLGENANVVR IMSIHKSKGL
     EFPVVICSAM GKNFNTQDFK KSILYHHNLG YGPQFVDYER RISFPSIAKE ALKSKINIEN
     LSEEMRVLYV AFTRAKEKLI ITGSTRNIQD SIKRWSNGIE SLDTISQYEI LKGKNFLDWI
     MPCVLRHRDL SNLLEEVGLD AVFNVEHNSK WYGKLWNKND ILVEKKSDEE KESIEEILEK
     IDVNNPDSDY YGEIEEKLNY IYPYEFSTRK PATISVTEIK KIQNNYEEEL INTIFEQKVI
     LKKPLFIQNE EEREKISGTE RGTIVHLVME VLDLKNVSSV NDIKSQIRGF VSKGIITEKQ
     ASIVNPYKIY KFFASNIGKR MLNAEIINRE KSIYAQVNMK DIYIYEKLIN NDDKKLYDNE
     SVMLRGIVDA YFEEDNQIVL VDYKTDFVNE ENINQIIEKY KKQLDLYADI IETLTGKSVK
     EKCIYLFGVD EAVCY