ID   ADDA_STAEQ              Reviewed;        1218 AA.
AC   Q5HQJ4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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}; Synonyms=rexA;
GN   OrderedLocusNames=SERP0555;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW53934.1; -; Genomic_DNA.
DR   RefSeq; WP_002486063.1; NC_002976.3.
DR   AlphaFoldDB; Q5HQJ4; -.
DR   SMR; Q5HQJ4; -.
DR   STRING; 176279.SERP0555; -.
DR   EnsemblBacteria; AAW53934; AAW53934; SERP0555.
DR   KEGG; ser:SERP0555; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000000531; 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..1218
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379323"
FT   DOMAIN          9..474
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          491..785
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1218 AA;  142368 MW;  E2ED050DE4EA8A7B CRC64;
     MIPTKPHDVI WTDAQWQSIY AKGQDILVAA AAGSGKTAVL VERIIQRILR DDVDVDRLLV
     VTFTNLSARE MKHRVDKRIQ EASFKDPNNE HLKNQRIKIH QAQISTLHSF CLKLIQQHYD
     VLDIDPHFRT SSEAENILLL EQTIDDVLEQ HYDKLDPHFI ELTEQLSSDR NDDQFRSIIK
     QLYFFSIANP QPFEWLNQLA QPYKEENKQQ QLMQLINDLA MIFMKAGYEE LQKSYDLFSM
     MESVDKQLEV IETERMFITK AIEGKVLNTD VITQHEFMSR FPAINSKIKE ANEGMEDALN
     EAKQHYDKYK SLVMKVKNDY FSRNAEDLQR DMQQLAPRVA YLAQIVQDVI QSFGVQKRSR
     NILDFSDYEH FALRILTNED GSPSRIAETY REHFKEILVD EYQDTNRVQE KILSCIKTGE
     EHDGNLFMVG DVKQSIYKFR QADPSLFIEK YNRFSSSGNE SGLRIDLSQN FRSRQEVLST
     TNYLFKHMMD EQVGEISYDD AAQLYFGAPY DEVSHPVQLR ALVEASSENS DLTGSEQEAN
     YIVEQVKDII NHQNVYDMKT GQYRKATYKD IVILERSFGQ ARNLQQAFKN NDIPFHVNSK
     EGYFEQTEVR LVLSFLRTID NPLQDIYLVG LMRSVIYQFT EEELAEIRVV SPHDDYFYQS
     IKNYMIDEKA DSRLVDKLNR FIQDIQKYQN YSQSQPVYQL IDKFYNDHFV IQYFSGLIGG
     KGRRANLYGL FNKAVEFENS SFRGLFQFIR FIDELIDRKK DFGEENVVGP NDNVVRMMTI
     HSSKGLEFPF VIYSGLSKKF NKGDLNAPVI LNQQYGLGMD YFDVNKDMAF PSLASVAYRA
     INEKELISEE MRLIYVALTR AKEQLILVGR VKDEKSLIKY EQLAVSDTHI AVNERLTATN
     PFVLIYGVLA KHQSPSLPND QRFERDIDQL NSEVKPRVSI VIDHYEDVST EEVVNDNEIR
     TIEELKAINT GNEDVKIKIH QQLSYDYPFK VNTMKPSKQS VSELKRQLET EESNTNYDRV
     RQYRIGVASY ERPKFLTQTK KRKANEIGTL MHTVMQHLPF REQRLTKDEL FQYIDRLIDK
     QLIDEDAKED IRIDEIMHFI DGPLYMEIAQ ADNVYTELPF VVNQIKVDGL TSEDEDVSII
     QGMIDLIYES DGQFYFVDYK TDAFNRRKGM SDEEIGNQLK EKYQIQMTYY RNTLETILKR
     PVKGYLYFFK FGTLEIDD