ADDA_BACCQ
ID ADDA_BACCQ Reviewed; 1241 AA.
AC B9ITE9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=BCQ_1201;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM11631.1; -; Genomic_DNA.
DR RefSeq; WP_000572276.1; NC_011969.1.
DR AlphaFoldDB; B9ITE9; -.
DR SMR; B9ITE9; -.
DR EnsemblBacteria; ACM11631; ACM11631; BCQ_1201.
DR KEGG; bcq:BCQ_1201; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000441; 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_0000379238"
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; 142759 MW; 22A4554C45D115EC CRC64;
MIENWPKKPE 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
YNEDVVKQVD SLRNKAKDEV KKLQEELFSR KPESFLRDFQ DMHPVLEKLV QLVKVFTERF
QAMKRDKGMV DFTDLEHFCL QILSEQSEEG 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 VKDATKEMEK
WLDAREHSEW LLPDHIRAGA SCYLDWIAPS LYRHRDSEIL LELGQGSVPD EIYGYDTSWK
VEVVDGNTLL APEPVQEEKQ ELLEALREKK AVPLESERKE EVYDRLMWKY GYEEATSHRA
KQSVTEIKRN YQSEEGSDNA FIKKLRAPIR TRPRFMEKKG LTYAERGTAV HAVMQHVDLK
KPITEEVIRE QIAGMVNKEL LTFEQAEEIA IEKVISFFDS DLGKRVLAAK SVEREVPFTM
MLAAEEAYQD WQGQSGESIL VQGVIDCMIE EEDGITLIDF KTDTIEGKFP GGFEQAKPIL
EERYKVQLSL YAKALEKSLQ HPVKEKCLYF FDGNHVVKIE E
