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ADDA_BACC1
ID   ADDA_BACC1              Reviewed;        1241 AA.
AC   Q73C23;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, 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}; OrderedLocusNames=BCE_1245;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS40174.1; -; Genomic_DNA.
DR   RefSeq; WP_000970454.1; NC_003909.8.
DR   AlphaFoldDB; Q73C23; -.
DR   SMR; Q73C23; -.
DR   PRIDE; Q73C23; -.
DR   EnsemblBacteria; AAS40174; AAS40174; BCE_1245.
DR   GeneID; 59159576; -.
DR   KEGG; bca:BCE_1245; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000002527; 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_0000379234"
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;  142702 MW;  6C597AF13AD489D3 CRC64;
     MMENWPKKPE GSQWTDDQWK AVVANGRDIL VAAAAGSGKT AVLVERIIKK IINEENPVDV
     DRLLVVTFTN AAAQEMKNRI GEALEKVLID EPGSQHIRKQ LSLLNKASIS TIHSFCLQVI
     RGYYYMLDVD PRFRIANQTE NELLKEEVLD DILEEEYGIE DNTIFFELVD RYTSDRSDDD
     LQRMILALHT ESRAHPNPEK WLDKLVEAYD VEGKTIEDLV YASYLLEDVK FQLETAEQHI
     RKATELAMLP DGPAPRVETL QADLALLGTL SSAARESWTS VYEAMQNVSW QTLKRIKKSD
     YNEDIVKQVD SLRNKAKDEV KKLQEELFSR KPESFLRDFQ DMHPVLEKLV QLVKVFTERF
     QAMKRDKGMV DFTDLEHFCL QILSEQSENG EMKPSAVALQ YRNKFAEVLV DEYQDTNFVQ
     ESIIKFVTKD SESEGNLFMV GDVKQSIYRF RLAEPGLFLG KYKRFTQEGL GGGMKIDLAK
     NFRSRHEVLA GTNFIFKQIM GEEVGEIDYD ADAELKLGAS YPEGEDVAAE LLCIQQTEEE
     VIDGEEGAEV EKAQLEARLM AQRIKAMVDS GYEVYDRKTD SMRPVQYRDF VILLRSMPWA
     PQIMEELKLQ GIPVYADLAT GYFEATEVNI MMNVFRVIDN PMQDIPLAAV LRSPIVGLND
     EELATLRAHG KKGSFYEVMS SFLKGAPLEE EKELHDKLEW FYNLLQGWRE FARQQSLSDL
     IWKVYGETGY YDFVGGLPAG KQRQANLRVL YDRARQYEAT SFRGLFRFLR FIERILERGD
     DMGTARALGE QEDVVRIMTI HKSKGLEFPV VFVAGLGRRF NTQDLMKRFL LHKDFGFGSQ
     FIDPRKRIKY TTLSQLAIKR KMKMELIAEE MRVLYVALTR AKEKLILIGT VKDANKEMEK
     WLDAREHSEW LLPDHIRAGA SCYLDWIAPS LYRHRDSEIL LELGQGSIPD EIYGYDTSWK
     VEVVDGNTLL APEPVQEEKQ ELLEALREKK AVPLQSERKE EVYDRLMWKY GYEEATSHRA
     KQSVTEIKRN YQSEEGSDNA FIKKLRAPIQ TRPRFMEKKG LTYAERGTAV HAVMQHVDLK
     KPITEEVIRE QIAGMVNKEL LTFEQAEEIA IEKVISFFDS DLGKRVLAAK SVEREVPFTM
     MLAAEEAYQD WQGKSGESIL VQGVIDCMIE EEDGITLIDF KTDTIAGKFP GGFDQAKPIL
     EERYKVQLSL YAKALEKSLQ HPVKEKCLYF FDGNHVVKIE E
 
 
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