ADDA_CLOBB
ID ADDA_CLOBB Reviewed; 1243 AA.
AC B2THC8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=CLL_A0025;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
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 sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001056; ACD24582.1; -; Genomic_DNA.
DR RefSeq; WP_012425324.1; NC_018648.1.
DR AlphaFoldDB; B2THC8; -.
DR SMR; B2THC8; -.
DR PRIDE; B2THC8; -.
DR EnsemblBacteria; ACD24582; ACD24582; CLL_A0025.
DR KEGG; cbk:CLL_A0025; -.
DR PATRIC; fig|935198.13.peg.16; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000001195; 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..1243
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379251"
FT DOMAIN 4..477
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 512..810
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 1243 AA; 144182 MW; 0E0C531AD31A3DF0 CRC64;
MSGTKWTEEQ LSAITTRDCN LLVAAAAGSG KTAVLVERII KIITNEENPI DIDKLLVVTF
TSAAAAEMRE RIANAISKKL DETPTSKNLQ KQLTLLNRSN IMTIHSFCLG VIKNNFHKID
LDPSFRICDQ TEGILLKMEI IDELFDDKYD EENQEFIKFI EAFSSYKSDN ALKELVLSLY
NFTMAGPWPK KWLKDASRDF DIKTLQELDE TKWVNVLKES IKIELDGYIK MMQKAVKLIN
ETDGLEPYFE GFSSELDLIV NAYNNVESSL NDLYNSLNLI TFNRLKTIKK NTVSDENIQN
LVKQIRDQVK KKISALIEGT FIASPDKMLD NIIKSYPYIN QLTELTSEFI DRFTAKKKEK
NILDFNDLEH LCLKILIEEN EENQIVPSTI AQKFKDYFEE VLVDEYQDSN NVQEAIIELV
SRKNSDNPNV FMVGDVKQSI YKFRQAKPEL FIDKYNSYSL DKGINRKIQL YKNFRSREEI
INGVNYIFKS VMSKTVGELE YTDVEALNLG ANYPEKKNDD DIIGGPIEVH ILDRSDNKEE
NDEFKLQAEE EIGDVNLEAR IIVKRINELI SKKEGNKFKV LDKDTGEYRD LKYKDIVILL
RATKNWSEVL LDELGLAGIP VYADTGSGYF ESIEIRTIMS LLKVIDNPMQ DVPMLSLLIS
PIIGLSAEEL SDIRLIDKEK YFYENIIKIS KEKLISVELQ EKCEYILSSI DKWRRKSIYM
PIDEFIWYLY MDTAYYGYVG AMPNGVLRQA NLKILFQRAR QFSDTSFKGL FNFINFINKL
TKSSGDMGSA KILGENEDVI RIMSIHKSKG LEFPVVFLAG CGKNFNLMDL NNKILYHEEL
GLGPEYINLE NRTSITTLPK EAIKKRMKLE TLSEEMRVLY VAFTRAKEKL IITGAVRNAE
KSIEKWINSA VLDKDVVLPY EISKGKSYLD WIGMALCKHK DGEILRKKLG FSSEMCKDDL
SMWKISIWNK YELDMYDELD ENQEEEDVKI SILDKDVNKE IKSEVYRRLG YEYEFKESTK
LTSNISVSDL KKRNIEDDID TLKMFDLEEE DNKNKDIITP KFLQEEKGIS AAERGTAIHF
AMKKIDFSKV GTLKEIKEQL NKLYDEELIL QEEYNSINPY KILSFFKSSL GKKMLYVYNE
GGKVYREVPF YTEISSLEID ESLPQKYANE KIRLQGIIDC FFKCDDEIIL LDYKTDYVEN
EEEFKDKYKN QLSYYSEAIF KMTGKKVDKK YLYSFYLEKE ILI
