ID   ADDA_STAA8              Reviewed;        1217 AA.
AC   Q2FZT5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
GN   OrderedLocusNames=SAOUHSC_00905;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (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; CP000253; ABD30030.1; -; Genomic_DNA.
DR   RefSeq; WP_000154930.1; NZ_LS483365.1.
DR   RefSeq; YP_499458.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZT5; -.
DR   SMR; Q2FZT5; -.
DR   STRING; 1280.SAXN108_0962; -.
DR   EnsemblBacteria; ABD30030; ABD30030; SAOUHSC_00905.
DR   GeneID; 3921751; -.
DR   KEGG; sao:SAOUHSC_00905; -.
DR   PATRIC; fig|93061.5.peg.826; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   PRO; PR:Q2FZT5; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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..1217
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379317"
FT   DOMAIN          10..475
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          476..786
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1217 AA;  141261 MW;  C61C2EE8A5A22412 CRC64;
     MTIPEKPQGV IWTDAQWQSI YATGQDVLVA AAAGSGKTAV LVERIIQKIL RDGIDVDRLL
     VVTFTNLSAR EMKHRVDQRI QEASIADPAN AHLKNQRIKI HQAQISTLHS FCLKLIQQHY
     DVLNIDPNFR TSSEAENILL LEQTIDEVIE QHYDILDPAF IELTEQLSSD RSDDQFRMII
     KQLYFFSVAN PNPTNWLDQL VTPYEEEAQQ AQLIQLLTDL SKVFITAAYD ALNKAYDLFS
     MMDSVDKHLA VIEDERRLMG RVLEGGFIDI PYLTGHEFGA RLPNVTAKIK EANEMMVDAL
     EDAKLQYKKY KSLIDKVKSD YFSREADDLK ADMQQLAPRV KYLARIVKDV MSEFNRKKRS
     KNILDFSDYE HFALQILTNE DGSPSEIAES YRQHFQEILV DEYQDTNRVQ EKILSCIKTG
     DEHNGNLFMV GDVKQSIYKF RQADPSLFIE KYQRFTIDGD GTGRRIDLSQ NFRSRKEVLS
     TTNYIFKHMM DEQVGEVKYD EAAQLYYGAP YDESDHPVNL KVLVEADQEH SDLTGSEQEA
     HFIVEQVKDI LEHQKVYDMK TGSYRSATYK DIVILERSFG QARNLQQAFK NEDIPFHVNS
     REGYFEQTEV RLVLSFLRAI DNPLQDIYLV GLMRSVIYQF KEDELAQIRI LSPNDDYFYQ
     SIVNYINDEA ADAILVDKLK MFLSDIQSYQ QYSKDHPVYQ LIDKFYNDHY VIQYFSGLIG
     GRGRRANLYG LFNKAIEFEN SSFRGLYQFI RFIDELIERG KDFGEENVVG PNDNVVRMMT
     IHSSKGLEFP FVIYSGLSKD FNKRDLKQPV ILNQQFGLGM DYFDVDKEMA FPSLASVAYR
     AVAEKELVSE EMRLVYVALT RAKEQLYLIG RVKNDKSLLE LEQLSISGEH IAVNERLTSP
     NPFHLIYSIL SKHQSASIPD DLKFEKDIAQ IEDSSRPNVN ISIVYFEDVS TETILDNDEY
     RSVNQLETMQ NGNEDVKAQI KHQLDYRYPY VNDTKKPSKQ SVSELKRQYE TEESGTSYER
     VRQYRIGFST YERPKFLSEQ GKRKANEIGT LMHTVMQHLP FKKERISEVE LHQYIDGLID
     KHIIEADAKK DIRMDEIMTF INSELYSIIA EAEQVYRELP FVVNQALVDQ LPQGDEDVSI
     IQGMIDLIFV KDGVHYFVDY KTDAFNRRRG MTDEEIGTQL KNKYKIQMKY YQNTLQTILN
     KEVKGYLYFF KFGTLQL