ID   ADDA_BACCN              Reviewed;        1242 AA.
AC   A7GM37;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Bcer98_0860;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
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; CP000764; ABS21195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7GM37; -.
DR   SMR; A7GM37; -.
DR   STRING; 315749.Bcer98_0860; -.
DR   PRIDE; A7GM37; -.
DR   EnsemblBacteria; ABS21195; ABS21195; Bcer98_0860.
DR   KEGG; bcy:Bcer98_0860; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000002300; 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..1242
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379240"
FT   DOMAIN          13..486
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          506..806
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1242 AA;  143918 MW;  24771631CD8E7573 CRC64;
     MMVENWPAKP EGSQWTDDQW KAVVAHGRDI LVAAAAGSGK TAVLVERIIK KIINEENPVD
     VDRLLVVTFT NAAAQEMKNR IGEALEKVLI EEPSSRHIRK QLSLLNKASI STIHSFCLQV
     IRSYYYMLDI DPRFRIANQT ENELLKEEVL DDILEEEYGM EENQLFFELV DRYTSDRNDD
     DLQRMILALH TAAGAHPNPE KWLDRLVEAY NVEGKTIEDL MYASYLLEDV KFQLETATEH
     IRKAMELAML PDGPAPRMET LQTDLVLLET LSHAARKSWT SVYEAMQHVS WQTLKRIKKS
     DYNEDIVKQV DSLRNKAKDE VKKLQEELFS RKPESFLRDF QEMHPVLGKL VQLVKEFSNR
     FQAIKRDKGM VDFTDLEHFC LQILSEQGED GELRPSPVAL QYRNRFAEVL VDEYQDTNFV
     QESIIKLVTK DSEQEGNLFM VGDVKQSIYR FRLAEPGLFL GKYKRFTQEG LEGGMKIDLA
     KNFRSRHEVL AGTNFIFKQI MGEEVGEIEY DADAELKLGA SYPEGEDVAA ELLCIHQSEE
     EVLDGEEGEE VEKAQLEARL IAQRIKAMVD SGYTVYDRKT NEMRQVQYRD FVILLRSMPW
     APQIMEELKL QGIPVYAELA TGYFEATEVN IMMNVFRVID NPVQDIPLAA VLRSPIVGLN
     DEELAMLRAH AKKGSFYEVM RSFLRGAPLE GGKELHEKLK WFYHLLQGWR EFARQQSLSD
     LIWKVYRETG YYDFVGGLPG GKQRQANLRV LYDRARQYEA TSFRGLFRFL RFIERILERG
     DDMGTARALG EQEDVVRIMT IHKSKGLEFP VVFVAGLGRR FNTQDLMQRF LLHKDFGFGS
     QFIDPRKRIK YTTLSQLAIK RKMKRELIAE EMRVLYVALT RAKEKLILIG TVKDKEKEME
     KWLDTREHTE WLLPDYVRAS ASCYLDWIAP SLYRHRDSEI LLELGQGTIP NEIYEYDTSW
     KVEFVDGKTL LAPEPAQEEK QELLEALREK KAVPLESERK DEVYNRLTWK YEYEDATLQR
     AKQSVTEIKR NYQSEDGSDT AFIQKLRAPI RTRPRFMEKK GLTYAERGTA VHAVMQHVDL
     KQSITIESIQ EQIAKMVNKE ILTFEQAEEI SVERIVAFFE SHLGKRVLEA KSVEREVPFT
     MMLSAKEAYQ NWQGKSEETI LVQGVIDCMI EEDDGITLID FKTDTIEGKF PGGFDQAKPI
     LEERYKVQLS LYAKALEKTL QHPVKEKCLY FFDGNHVITI EE