ID   ADDA_STAHJ              Reviewed;        1225 AA.
AC   Q4L4Y3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=SH1983;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006716; BAE05292.1; -; Genomic_DNA.
DR   RefSeq; WP_011276250.1; NC_007168.1.
DR   AlphaFoldDB; Q4L4Y3; -.
DR   SMR; Q4L4Y3; -.
DR   STRING; 279808.SH1983; -.
DR   EnsemblBacteria; BAE05292; BAE05292; SH1983.
DR   KEGG; sha:SH1983; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000000543; 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..1225
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379324"
FT   DOMAIN          11..478
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          479..790
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   REGION          999..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1225 AA;  144123 MW;  2391D6AC685B8D5F CRC64;
     MNNIPIKPKD AQWTDAQWKS IYANGQDVLV AAAAGSGKTA VLVERIIQKI IRDEIDVDKL
     LVVTFTNLSA REMKHRVDQR IQQASIEDPR NEHLKNQRIK IHQAQISTLH SFCLKIIQQH
     YDVIDLDPNF RTISDVENVL LLEQSIDEVL EKHYDTPDIE FLTLVEQLSS DRNDDNFRDL
     LKRFYNFSIA NPSPFEWLDS LVEIYTDDNK HKLYLDELER LSKIYIKAAY HTLLEAENNF
     LNCIEAEKHL DVIKLEKFKC EKMIEGNVIN FEEIINYTSE KLPTITKKLK DTNEDEGISS
     QFLTNAKDFF DDYKKLLSEV KNKYLMRSYE DLKVDMKRLA PRIQYLVQIV KDIINGFAEK
     KRSRNVLDFS DYEHFALQIL TDQEGNASPI AKEYRSQFEE ILVDEYQDTN QVQEAIISKI
     KRGDESNGNL FMVGDVKQSI YKFRQADPTL FMDKYHRFTK DGDQSGLRID LSKNFRSRKE
     VLATTNYLFD HMMDEEVGEI EYDADARLYF GATKYSDKSM PLELHALIQD KSSDNDLEKS
     EQEARYIAEQ VKYIIEHKQV YDMKSETYRQ ATFKDIVILE RGLKNARNLQ QVFKDYNIPF
     HVNSKEGYFE QTEVRLVLSF LRTVDNPLQD IYLVGLMRSV IYQFTEDELA NIRVQSMNDD
     YFYQSILHYM KDQEANPLLV EKLEHFMDDI NMYQEYSQSH PVYQLIDKFY NDHYVIQYFS
     GLIGGKGRRA NLYGLFNKAV EFENSSFRGL YQFIRFIDEL IERNKDFGEE NVIGPNDNVV
     RMMTVHSSKG LEFPYVIYSE LSKNFNKGDL RKPLILNQKY GLGIDYFDLE QNVTYPSLSS
     VVIKSITEKE LISEEMRLMY VALTRAKEQL ILIGTIDKEE ALEKLERLPI SGNQIALHKR
     LSADRPFDLI YSILAKYQST SLLPEYRFEK SIDNLDESLR PTVDIKIAQF EELSIEDSES
     EQESRNISDL EVEGSHDDTL KQQINDQLSF KYPYLKDTEK PSKQSVSELK RQLETEESGT
     SYERVRQYRI GVSTYERPKF LRENKKRKAN EIGTLMHTVM QHLPFKETRM TETELNDYIN
     ELIEKHIIEE DAKKDIQFEA VMNFIRSDLY MTITQADKVY RELPFVVNQA RVDEMPESDE
     DVSIIQGMID LIFLKDDQYY FVDYKTDAFN KRRGMTDEEV GIQLRDKYKI QMKYYKNTLE
     TILNSKVYGY LYFFQFGQMS IEEDV