ID   ADDA_BACMK              Reviewed;        1241 AA.
AC   A9VJ02;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
GN   OrderedLocusNames=BcerKBAB4_1041;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY42291.1; -; Genomic_DNA.
DR   RefSeq; WP_012260538.1; NC_010184.1.
DR   AlphaFoldDB; A9VJ02; -.
DR   SMR; A9VJ02; -.
DR   STRING; 315730.BcerKBAB4_1041; -.
DR   EnsemblBacteria; ABY42291; ABY42291; BcerKBAB4_1041.
DR   KEGG; bwe:BcerKBAB4_1041; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000002154; 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..1241
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379245"
FT   DOMAIN          12..485
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          505..805
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   1241 AA;  142744 MW;  AE6D1CB2A058EC2B CRC64;
     MIENWPQKPE GSQWTDDQWK AVVANGRDIL VAAAAGSGKT AVLVERIIKK IIREENPVDV
     DRLLVVTFTN AAAQEMKNRI GEALEKVLID GPGSQHIRKQ LSLLNKASIS TIHSFCLQVI
     RGYYYMLDVD PRFRIANQTE NELLKEEVLD DILEEEYGIE DNSIFFELVD RYTSDRSDDD
     LQRMILALHT ESRAHPNPEK WLDKLVEAYD VEGKTIEDLV YASYLLEDVK FQLETAEKHI
     RKATELAMLP DGPAPRVETL QADLALLGTL SSAARGSWTS VYEAMQNVSW QTLKRIKKSD
     YNEDVVKRVD SLRNKAKDEV KKLQEELFSR RPESFLRDFQ DMHPVLEKLV KLVKVFTERF
     QAIKRDKGMV DFTDLEHFCL QILSEQSEDG EMKPSAVALQ YRNKFAEVLV DEYQDTNFVQ
     ESIIKFVTKD FESEGNLFMV GDVKQSIYRF RLAEPGLFLG KYKRFTQEGS GGGMKIDLAK
     NFRSRHEVLA GTNFIFKQIM GEEVGEIDYD ADAELKLGAS YPEGEDVAAE LLCIQQTEEE
     VQDGEEGAEV EKAQLEARLM AQRIKAMVDS GYAVYDRKTD SMRPVQYRDF VILLRSMPWA
     PQIMEELKLQ GIPVYADLAT GYFEATEVNI MMNVFRVIDN PMQDIPLAAV LRSPIVGLND
     EELATLRAHG KKGSFYEVMS SFLKGAPLEE EQELHDKLEW FYKLLQGWRE FARQQSLSDL
     IWKVYGETGY YDFVGGLPAG KQRQANLRVL YDRARQYEAT SFRGLFRFLR FIERILERGD
     DMGTARALGE QEDVVRIMTI HKSKGLEFPV VFVAGLGRRF NTQDLMKRFL LHKDFGFGSQ
     FIDPRKRIKY TTLSQLAIKR KMKMELIAEE MRVLYVALTR AKEKLILIGT VKDANKEMEK
     WLDAREHSEW LLPDHIRAGA SCYLDWIAPS LYRHRDSEML LELGQGNIPG EIYEYSASWK
     VEVVEGKDLL APEPVQEEKQ ELLEALRDKK AVPLESERKE EVYDRLMWKY GYEDATSHRA
     KQSVTEIKRN YQSEEGSDNA FIKKLRAPIK TRPRFMEKKG LTYAERGTAV HAVMQHVDLK
     KPITIEVLQE QIARMVNKEL LTFEQAEEIA IEKVISFFDS DLGKRVLAAK SVEREVPFTM
     MLSAEEAYQD WQGKKGESIL VQGVIDCMIE EEDGITLIDF KTDTIEGKFP GGFDQAKPTL
     EDRYKVQLSL YAKALEKSLK HPVKEKCLYF FDGNHVVNIE E