ID   ADDA_STAAR              Reviewed;        1217 AA.
AC   Q6GIC1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=SAR0929;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39935.1; -; Genomic_DNA.
DR   RefSeq; WP_000154950.1; NC_002952.2.
DR   AlphaFoldDB; Q6GIC1; -.
DR   SMR; Q6GIC1; -.
DR   KEGG; sar:SAR0929; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000000596; 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..1217
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379311"
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;  141287 MW;  4C39CB4FDF8DF4A9 CRC64;
     MTIPEKPQGV IWTDAQWQSI YETGQDVLVA AAAGSGKTAV LVERIIQKIL RDGIDVDRLL
     VVTFTNLSAR EMKHRVDQRI QEASIADPAN AHLKNQRIKI HQAQISTLHS FCLKLIQQHY
     DVLNIDPNFR TSSEAENILL LEQTIDEVIE QHYDILDPAF IELTEQLSSD RSDDQFRMII
     KQLYFFSVAN PNPTNWLDQL VTPYEEEAQQ AQLIQLLTDL SKVFITAAYD ALNKAYDLFS
     MMDGVDKHLA VIEDERRLMG RVLEGGFIDI SYLTGHEFGA RLPNVTAKIK EANEMMVDAL
     EDAKLQYKKY KSLIDKVKSD YFSREADDLK ADMQQLAPRV KYLARIVKDV MSEFNRKKRS
     KNILDFSDYE HFALQILTNE DGSPSEIAES YRQHFHEILV DEYQDTNRVQ EKILSCIKTG
     DEHNGNLFMV GDVKQSIYKF RQADPSLFIE KYQRFTLDGD GTGRRIDLSQ NFRSRKEVLS
     TTNYIFKHMM DEQVGEVRYD EAAQLYYGAP YDESDHPVNL KVLVEADQEH SDLTGSEQEA
     HFIVEQVKDI LEHQKVFDMK 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 FPSLASVAYK
     AVAEKKLVSE EMRLVYVALT RAKEQLYLIG RVKNDKSLLE LEQLSISGEH IAVNERLTSP
     NPFHLIYSIL SKHQSASIPD DLKFEKDIAQ IEDSSRPNVN ISIIYFEDVS TETILDNDEY
     RSVNQLETMQ NGNEDVKAQI KHQLDYQYPY VNDTKKPSKQ SVSELKRQYE TEESGTSYER
     VRQYRIGFST YERPKFLSEQ GKRKANEIGT LMHTVMQHLP FKKERISEVE LHQYIDGLID
     KHIIEADTKK DIRMDEIMTF INSELYSIIA EAEQVYRELP FVVNQALVDQ LPQGDEDVSI
     IQGMIDLIFV KDGVHYFVDY KTDAFNRRRG MTDEEIGTQL KNKYKIQMKY YQNTLQTILN
     KEVKGYLYFF KFGTLQL