ID   ADDA_LACDB              Reviewed;        1227 AA.
AC   Q04AN7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=LBUL_0908;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000412; ABJ58485.1; -; Genomic_DNA.
DR   RefSeq; WP_011678227.1; NC_008529.1.
DR   AlphaFoldDB; Q04AN7; -.
DR   SMR; Q04AN7; -.
DR   PRIDE; Q04AN7; -.
DR   KEGG; lbu:LBUL_0908; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   BioCyc; LDEL321956:LBUL_RS04335-MON; -.
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..1227
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379280"
FT   DOMAIN          3..477
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          505..788
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         24..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1227 AA;  138825 MW;  4B13E197CDD1D791 CRC64;
     MAVKYTPDQA RAIESRGQDL LVSASAGSGK TSVLVERVIR EIMDDHLEVN QLLVITFTRA
     AASEMKQRIK QRLQDRLQEE TDASQADFLR RQLAEIDTAI ISTIDSFCLD VIRRFYFAID
     IDPDFSILTD ATQIELLKER ALRDVENGYL QNEDQAKKDR FLALYDAFAG DSNANSARDL
     LFDLYQFAMA RPNYRAWLQK LAAPYQLETS DVVDSTLWQE KIKPYLEEEF SNLADKLTAL
     MAEADFDHEK FAKYQPAFTA FATSLASYRE SLATDDPFDR QRELLAACQF DGTLRTNKEI
     ADFVEEAKEV KEAGKQLVFN VYTSFYASSN ADQHALLAKG AEIASAAAEV ELAFIDRFNE
     LKRADRVLDF SDMEQLAYEI LTQDSSNSDL ARAYYQSRFK EIMVDEYQDT NALQDGLIQR
     LKKAGKNNLF MVGDVKQSIY GFRQAEPSLF IAKYDEYGQE NSAGKQRIIF AENFRSSQPV
     TQAVNLIFDS LLTKDFGGID YQKEGQLKFA AGYDPEAALP TETEVLYQED SSATDDDGEL
     NQGDLAMVIS RIQKLIADQT PIFDPKTGQT RPVSYGDIAI LTRSKTSNLD IKQEFDRYGV
     PLFVMDVQNY FQTFELTVIM SYLKIIDNPD QDIPLVAVLR SPIFNFSSSD LAEIRLVNKS
     VSFYAALRTY AKKDTDLAAR CRDFLAQLQD LRDFSLSHRI SELLWTIYER TSFLEIVTAM
     TNGQQRRLNL TALYERASAY ESSGFKDLYQ FINFIARMRK NQKDLAQPIL SENAGNSVKL
     MTIHASKGLE FPVVFVLGLE HRYNYQQDIT GSYVLDASGL GLSFAYPFDE AEYRADTLAN
     AWLKIAKKKK LLEEEARLLY VALTRAKQKL ILAANIKLPA RTDLAGLEEK WAKEISAGRL
     TLLDKMKVAK PLDFLAPALA RAKQVKRLGE KAVSDLATGQ EGSLVFVHFD PKKDQAQLPD
     SEAVAASGAD LTEDEAAVFK QAEKLYTFSQ GGYPYLDASR TTAYQAVSEI KKVFGDPIED
     ELADSHISEL QSANRYLQPI DTEPDFLFQN TVSSAELGTA SHLVLQYYDY AKGDKDAIDS
     CIAGLVEKGR LSQTLASMLD REALSWFVKS DFAKDFYQQP DRLHREENFA TILSPKTLFK
     DFSDFPGKIL VHGTIDGYYE AENGIILFDY KTDHVNPRKQ DEAIQKLKEK YQGQLRLYER
     ALNESGRLPV LKKYLVLLSC REIVEVD