ADDA_CLOBA
ID ADDA_CLOBA Reviewed; 1244 AA.
AC B2UX57;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=CLH_0025;
OS Clostridium botulinum (strain Alaska E43 / Type E3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=508767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alaska E43 / Type E3;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL Submitted (MAY-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; CP001078; ACD53404.1; -; Genomic_DNA.
DR RefSeq; WP_012451314.1; NC_010723.1.
DR AlphaFoldDB; B2UX57; -.
DR SMR; B2UX57; -.
DR PRIDE; B2UX57; -.
DR KEGG; cbt:CLH_0025; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
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..1244
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379249"
FT DOMAIN 4..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 517..811
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1244 AA; 144092 MW; 53A01E8D4C675049 CRC64;
MSGTKWTEEQ LSAITTRDCN LLVAAAAGSG KTAVLVERII KIITNEENPI DIDKLLVVTF
TSAAAAEMRE RIANAISKKL DETPTSKNLQ KQLTLLNRSN IMTIHSFCLG VIKNNFHKID
LDPSFRICDQ TEGILLKMEI IDELFDDKYD EENQEFIKFI EAFSSYKSDN ALKELVLSLY
NFIMAGPWPK KWLKAASEDF DIKTLQELDE SKWVSVLKES IKIELDGYIK MMQKAVELIN
ETDGLEPYFE GFSSELDLIV NAYNNVESSL NDLYNSLNLI TFNRLKTIKK NTVSDENIQN
LVKQIRDQVK KKISALIEGT FIATPDKMLD NIIKSYPYIN QLTELTSEFI DRFNAKKKEK
NILDFNDLEH LCLKILIEDN EENQIVPSTI AQKFKDYFEE VLVDEYQDSN NVQEAIIELV
SRKNSDNPNV FMVGDVKQSI YKFRQAKPEL FIDKYNSYSL DKGINRKIQL YKNFRSREEV
INGVNYIFKS VMSKTVGELE YTDVEALNLG ASYPKKKNVD DIIGGPIEVH ILDRSDNKEE
NDESKLQAEE EEIGDVNLEA RIIVKRINDL ISKKDGSKFK VLDKDTGEYR DLKYKDIVIL
LRATKNWSEV LLDELGLAGI PVYADTGSGY FESIEIRTIM SLLKVIDNPM QDVPMLSLLI
SPIIGLSAEE LTDIRLIDKE KYFYENIIKI STEKLISEEL QEKCEYILSS IDKWRRKSIY
MPIDEFIWYL YMDTAYYGYV GAMPNGVLRQ ANLKILFQRA RQFSETSFKG LFNFINFINK
LTKSSGDMGS AKILGENEDV VRIMSIHKSK GLEFPVVFLA GCGKNFNLMD LNNKILYHEE
LGLGPEYINL ENRTSITTLP KEAIKKRMKL ETLSEEMRVL YVAFTRAKEK LIITGAVRNA
EKSIEKWINS AVLDKDVILP YEISKGKSYL DWIGMALCKH KDGKILRKKL GFSSEMCKDD
LSMWKISIWN KYELDMYDEL DENQEELDVK ISILDKDVNK KVKSEVYRRL GYEYEFKEST
KLTSNISVSD LKRRNMNDNI DTLEIFDLEE EDNKNKDVIT PKFLQEKKGI SSAERGTAIH
FAMKKIDFSK VGTLKEIKEQ LNKLYEEEFI LQEEYSSINP YKILSFFKSN LGKKMLDVYN
KGGKIYREIP FHTEISSLEL DESLPQKYAN EKIRLQGIID CFFKCDDEII LLDYKTDYVE
NEEEFKEKYK SQLLYYSEAV FKMTGKKVNK RYLYSFYLEK EILI
