ADDA_BACC2
ID ADDA_BACC2 Reviewed; 1241 AA.
AC B7IL84;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=BCG9842_B4148;
OS Bacillus cereus (strain G9842).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK96545.1; -; Genomic_DNA.
DR RefSeq; WP_000572302.1; NC_011772.1.
DR AlphaFoldDB; B7IL84; -.
DR SMR; B7IL84; -.
DR EnsemblBacteria; ACK96545; ACK96545; BCG9842_B4148.
DR KEGG; bcg:BCG9842_B4148; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000006744; 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_0000379237"
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; 142865 MW; 054C6131774F0A5C 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 DGPAPRVETL QADVALLGTL SSAARESWTS VYEAMQNVSW QTLKRIKKSD
YNEDVVKQVD SLRNKAKDEV KKLQEELFSR KPESFLRDFQ DMHPVLEKLV QLVKVFTERF
QAMKRDKGMV DFTDLEHFCL QILSEQSENG EMNPSAVAFQ YRNKFTEVLV DEYQDTNFVQ
ESIIKFVTKD SESEGNLFMV GDVKQSIYRF RLAEPGLFLG KYKRFTQEGL GGGMKIDLAK
NFRSRHEVLA GTNFIFKQIM GEEVGEIDYD ADAELKLGAT YPEGEDVAAE LLCIQQTEEE
VIDGEEGAEV EKAQLEARLM AQRIKAMVDS GYEVYDRKTD SMRPVQYRDF VILLRSMPWA
PQIMEELKLQ GIPVYADLAT GYFEATEVNI MMNVFRVIDN PMQDIPLAAV LRSPIVGLND
EDLATLRAHG KKGSFYEVMS SFLKGAPLEE EQELHEKLEW 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 EIYGYDTNWK
VEVVDGNTLL APEPVQEEKQ ELLEALREKK AVPLQSERKE EVYDRLMWKY GYEDATSYRA
KQSVTEIKRN YQSEEGSDNA FIKKLRTPIK TRPRFMEKKG LTYAERGTAV HAVMQHVDLK
KPITVEVLQE QIAGMVNKEL LTFEQAEEIA IEKVISFFDS DLGKRVLAAK SVEREVPFTM
MLAAEEAYQD WQGKSEETIL VQGVIDCMIE EEDGITLIDF KTDTIEGKFP GGFEQAKPIL
EDRYKVQLSL YAKALEKSLQ HPVKEKCLYF FDGNHVVNIE E
