ID   ADDA_BACCR              Reviewed;        1241 AA.
AC   Q81GP9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=BC_1138;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(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; AE016877; AAP08125.1; -; Genomic_DNA.
DR   RefSeq; NP_830924.1; NC_004722.1.
DR   RefSeq; WP_000572298.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81GP9; -.
DR   SMR; Q81GP9; -.
DR   STRING; 226900.BC_1138; -.
DR   PRIDE; Q81GP9; -.
DR   EnsemblBacteria; AAP08125; AAP08125; BC_1138.
DR   KEGG; bce:BC1138; -.
DR   PATRIC; fig|226900.8.peg.1101; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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..1241
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379235"
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;  142718 MW;  6FB309480CAEBBE2 CRC64;
     MIENWPKKPE GSQWTDDQWK AVVANGRDIL VAAAAGSGKT AVLVERIIKK IINEENPVDV
     DRLLVVTFTN AAAQEMKNRI GEALEKVLID EPGSQHVRKQ LSLLNKASIS TIHSFCLQVI
     RGYYYMLDVD PRFRIANQTE NELLKEEVLD DILEEEYGIE DNTIFFELVD RYTSDRSDDD
     LQRMILALHT ESRAHPNPEK WLDKLVEAYD VEGKTIEDLV YASYLLEDVK FQLETAEQHI
     RKATELAMLP DGPAPRIETL QADVALLGTL SSAARESWTS VYEAMQNVSW QTLKRIKKSD
     YNEDVVKQVD SLRNKAKDEV KKLQEELFSR KPESFLRDFQ DMHPVLEKLV QLVKVFTERF
     QAMKRDKGMV DFTDLEHFCL QILSEQSENG EMNPSAVALQ YRNKFAEVLV DEYQDTNFVQ
     ESIIKFVTKD SESEGNLFMV GDVKQSIYRF RLAEPGLFLG KYKRFTQEGL GGGMKIDLAK
     NFRSRHEVLA GTNFIFKQIM GEEVGEIDYD ADAELKLGAT YPEGEDVAAE LLCIQQTEEE
     VIDGEEGAEV EKAQLEARLM AQRIKAMVDS GYEVYDRKND SMRPVQYRDF VILLRSMPWA
     PQIMEELKLQ GIPVYADLAT GYFEATEVNI MMNVFRVIDN PMQDIPLAAV LRSPIVGLSD
     EELATLRAHG KKGSFYEVMS SFLKGAPLEE EQELHDKLEW FYNLLQGWRE FARQQSLSDL
     IWKVYGETGY YDFVGGLPAG KQRQANLRVL YDRARQYEAT SFRGLFRFLR FIERILERGD
     DMGTARALGE QEDVVRIMTI HKSKGLEFPV VFVAGLGRRF NTQDLMKRFL LHKDFGFGSQ
     FIDPRKRIKY TTLSQLAIKR KMKMELIAEE MRVLYVALTR AKEKLILIGT VKDANKEMEK
     WLDAREHSEW LLPDHIRAGA SCYLDWIAPS LYRHRDSEML LELGQGSIPD EIYGYDTSWK
     VEVVDGNTLL APEPVQEEKQ ELLEALREKK AVPLQSERKE EVYDRLMWKY GYEDATSHRA
     KQSVTEIKRN YQSEEGSDNA FIKKLRAPIK TRPRFMEKKG LTYAERGTAV HAVMQHVDLK
     KPITVEVLQE QIAGMVNKEL LTFEQAEEIA IEKVISFFDS DLGKRVLAAK SVEREVPFTM
     MLAAEEAYQD WQGKSEETIL VQGVIDCMIE EEDGITLIDF KTDTIEGKFP GGFEQAKPIL
     EDRYKVQLSL YAKALEKSLQ HPVKEKCLYF FDGNHVVNIE E