ADDA_BACC0
ID ADDA_BACC0 Reviewed; 1240 AA.
AC B7JDU4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=BCAH820_1220;
OS Bacillus cereus (strain AH820).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820;
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 AH820.";
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; CP001283; ACK89857.1; -; Genomic_DNA.
DR RefSeq; WP_000572289.1; NC_011773.1.
DR AlphaFoldDB; B7JDU4; -.
DR SMR; B7JDU4; -.
DR EnsemblBacteria; ACK89857; ACK89857; BCAH820_1220.
DR KEGG; bcu:BCAH820_1220; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001363; 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..1240
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379233"
FT DOMAIN 12..485
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 497..804
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 1240 AA; 142649 MW; 388859C397A31683 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 QADLALFGTL SAAARESWTS VYEAMQNVSW QTLKRIKKSD
YNEDIVKQVD SLRNKAKDEV KKLQEELFSR RPESFLRDFQ DMHPVLEKLV QLVKVFTERF
QAMKRDKGMV DFTDLEHFCL QILSEQSEDG EMKPSAVALQ YRNKFAEVLV DEYQDTNFVQ
ESIIKFVTKD SESEGNLFMV GDVKQSIYRF RLAEPGLFLG KYKRFTQEGL GGGMKIDLAK
NFRSRHEVLA GTNFIFKQIM GEEVGEIDYD ADAELKLGAS YPEGEDVAAE LLCIQQTEEV
IDGEEGAEVE KAQLEARLMA QRIKAMVDSG YEVYDRKTDS MRPVQYRDFV ILLRSMPWAP
QIMEELKLQG IPVYADLATG YFEATEVNIM MNVFRVIDNP MQDIPLAAVL RSPIVGLNDE
ELATLRAHGK KGSFYEVMSS FLKGAPLEEE KELHDKLEWF YNLLQGWREF ARQQSLSDLI
WKVYGETGYY DFVGGLPAGK QRQANLRVLY DRARQYEATS FRGLFRFLRF IERILERGDD
MGTARALGEQ EDVVRIMTIH KSKGLEFPVV FVAGLGRRFN TQDLMKRFLL HKDFGFGSQF
IDPRKRIKYT TLSQLAIKRK MKMELIAEEM RVLYVALTRA KEKLILIGTV KDATKEMEKW
LDAREHSEWL LPDHVRAGAS CYLDWIAPSL YRHRDSEMLL ELGQGSIPDE IYGYDTSWKV
EVVDGNTLLA PEPVQEEKQE LLEALREKKA VPLESERKEE VYDRLMWKYR YGEATSHRAK
QSVTEIKRNY QSEEGSDNAF IKKLRAPIRT RPRFMEKKGL TYAERGTAVH AVMQHVDLKK
PITVEVLQEQ IAGMVNKELL TFEQAEEIAV EKVISFFDSD LGKRVLAAKS VEREVPFTMM
LAAEEAYQDW QGKSGESILV QGVIDCMIEE EDGITLIDFK TDTIEGKFPG GFEQAKPILE
ERYKVQLSLY AKALEKSLQH PVKEKCLYFF DGNHVIKVEE
