ADDA_CLOBM
ID ADDA_CLOBM Reviewed; 1279 AA.
AC B1KUZ8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-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=CLK_3638;
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA55236.1; -; Genomic_DNA.
DR RefSeq; WP_012343244.1; NC_010520.1.
DR AlphaFoldDB; B1KUZ8; -.
DR SMR; B1KUZ8; -.
DR PRIDE; B1KUZ8; -.
DR EnsemblBacteria; ACA55236; ACA55236; CLK_3638.
DR KEGG; cbl:CLK_3638; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000000722; 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..1279
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379254"
FT DOMAIN 4..499
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 526..853
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 1279 AA; 150210 MW; CEA29FAB9A9AAC27 CRC64;
MSSTKWTDEQ RQAVFTKNCN LLVAAGAGAG KTAVLVQRII EKILDKEEPI DIDKLLVVTF
TNAAAAEMRE RIGDAISKGL DENPESKALR KQLTLLNKSN IMTIHSFCLQ IIKNNFHTIE
IDPNFRICDE TEGILMKQEA MDELFDELYE IENKDFINLV ESYASRKDTR LQEVVLELHR
FAKSAPFPYD WLLNMAEEFN VGEEFNFEET LWADMIMEDM KVLLHGFKNM LQQSIDVILN
SEGIDYYYEP FKMDLNFINS LLEKSSFKEF RGEIIAYDFP KLPLKRNKDA DKEAKERVKK
LRDRVKKKIL EIKNILNSYE NEFIKKEFIF LYPSMKALSN LVILFDKKYE AKKRERDLID
FNDIEHLCLS ILTDKDSEDH IIPSDTALDY RKKFTEVLID EYQDSNLVQE VIMSMVSRVK
GYWSFYNGQL MFNEEEINLE EPHIGLDIPN RFMVGDVKQS IYRFRQAKPE IFLDKYNEYS
EEESIKNRKV KLFKNFRSRE EVINGVNYLF KQIMSKTIGE LDYTEEEALK VGASYGEEVK
GEPIELCLMD KKYEISEEVL KEYNMDEEEA LDNIQLEGRL VAKKIQKLVG NNLEGGLKVF
DKKLGEYRNL QYRDIVILMR ATSNWAPVFV EELAKEGIPV FADTNSGYFN TTEIKTIISL
LQIIDNPLQD IPLLSVLRSP IASFTDDELI DIRMVNKNIA FYECMEIIYK LYKDEELDSY
YSFYMEDEDK TNKIVKDIKE ELKNKICSFI EKLNLWRKKS IHIDIDEFIW FLYVETGYYG
YVGALPAGEQ RQANLRILFQ RAKQYEKTSY KGLFNFINFI NKLKFSSGDM GSAKILGENE
NVVRIMSIHK SKGLEFPVVI LSGTGKNFNM MDLNKNILFH RDLGYGPDYV DTERRIAYPS
LVKNIIKNKI RLETLSEEMR ILYVALTRAR EKLIITGLIN NMDKTVEDWL NLSDDKNKVP
EYAVMSGKTY LDWIGPALIK HKDAVSLREE LKITSGLSNI VDDKSKWKIE LWNKKELLKE
KVEENEVEIS EKIKETLMNL GESNYKEEIY KKLSFKYKYD NASSIPTKLS VSDVKKQFIL
DEKENTEELF KKVELRKPMF MGEEKKISPS ERGTIIHLFM QHLDLKKAEN EEDIKEQINR
LIEREFITYE QSKIINPYKI LKFCRSELGK RMINSNNINR EMPFSIEVPA VEIYRELDKD
IYKDEKLIIQ GIIDCYFEEE EGLVLLDYKT DYVNDIEEIK NRYEIQIKYY EEALNRITGK
NVKDKYLYLF SVDNYIKID
