ID   ADDA_ENTFA              Reviewed;        1264 AA.
AC   Q836J8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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}; Synonyms=rexA;
GN   OrderedLocusNames=EF_1113;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80913.1; -; Genomic_DNA.
DR   RefSeq; NP_814843.1; NC_004668.1.
DR   RefSeq; WP_002416113.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q836J8; -.
DR   SMR; Q836J8; -.
DR   STRING; 226185.EF_1113; -.
DR   DNASU; 1200015; -.
DR   EnsemblBacteria; AAO80913; AAO80913; EF_1113.
DR   KEGG; efa:EF1113; -.
DR   PATRIC; fig|226185.45.peg.2382; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001415; 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..1264
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379270"
FT   DOMAIN          12..482
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          520..808
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1264 AA;  146451 MW;  6DEA770A76C4F5E7 CRC64;
     MSKTIPLRPA NEQFTDSQWQ AVFDGDENIL VSASAGSGKT TVLVRRVIEK VKSGVDIDRL
     LIVTYTEAAA REMKERIQVA LQKAMNEEQD PERRRHFSRQ IALLPTANIS TLHAFCLTVI
     RRFYYLIDID PVFRMLTDET ETLLLKEDVW DALREQFYAE NQEAFYQLTA NFSNDRSDDG
     LTNLIFSFYE FAKANPDPEA WINGLTQAYE VGDQLGESKL FQTYLKPLAV ETLQRTLQRY
     EEMVTLTEGE EKLQKIWYLA QNEKEQTKQF LQFLERNDLE SAYNLTELLS FDRYPTVRAE
     ELKPTAEQAK QLREQNKKAL NDLKKQLFTL SPDAMKQVLK EATPIVQEMA HVGKQFMEAY
     GAEKRLKNLV DFNDLEHYTL AILAKNQADG WHASEASVYY REKFDEVLVD EYQDINQLQE
     SILYWLRRPL STEGNLFMVG DVKQSIYSFR LADPTLFIEK YNQYGQGKEG KRIILAENFR
     SRKDVLDFTN LVFSQLMDER VGQIAYDESA ALVHGFDQFS EAADYSTELL IYEKKATESV
     EFPELQSPEL LIEDKTEGEL YVTALKIREL IDQNFLIYDK KLKTDRPITY QDIVLLTPTK
     KNNLTILDVF KSLEIPVQVN DAQNYFQATE IRTMIALLQL IDNPYQDIPL AAVLRSPIVG
     LKENELVLIR LANKETSYYE AFLTFNQKME PTMEEAVVQE KTIRFAESLE KWREQARRNQ
     ISNLLWTIYR ETAYLDYVGG LPVGKQRQAN LYALVDRAAA YEKTTFRGLF QFVRFIEKMQ
     EKDKDLAEPV VLSEENAVRV MTIHASKGLE FPVVFVLDMT KEFNVSDLNE RYIFEENLGV
     GIRYLQPEER VMYDTLPFLA IKQVRLRKLL SEEMRKLYVA LTRAEQKLFL VGSYKDQAAM
     WKEWLKVGDV ETLVLPAENR LQSKSSLMNW VGMTLVRHQK ADEYQQEVVV SNVPQVKKHP
     ANFHIQWFNE EQLRAAIQQL QLPERQAEDL AEKAQLSADK INRGLARLSF NYPFEVATRT
     TSYQSVSEIK RVFDDPDNKE IGKIEVREDN TIQAQPLIVN RMIEGDLSKP KFLDTVQAPS
     AAEIGTATHY LLQLIDLSKQ PSYEEVRAVQ ERLVENKLIL PAIAEKMNLE QIVAFFDTAL
     GKQLIQHHQT VRREQPFSML IEAEELIQNY PETTQDDLLI HGIIDGYIEL DNQCILYDYK
     TDHVKGTSPQ AISEIVERYR GQMNLYRRAL QEATHKEVSH VYLILLNGGV IIDMQTGNVV
     DFIK