ADDA_CLOBJ
ID ADDA_CLOBJ Reviewed; 1279 AA.
AC C1FSA8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-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}; OrderedLocusNames=CLM_0518;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
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; CP001581; ACO86963.1; -; Genomic_DNA.
DR RefSeq; WP_012705612.1; NC_012563.1.
DR AlphaFoldDB; C1FSA8; -.
DR SMR; C1FSA8; -.
DR STRING; 536232.CLM_0518; -.
DR EnsemblBacteria; ACO86963; ACO86963; CLM_0518.
DR KEGG; cby:CLM_0518; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001374; 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_1000185004"
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; 150199 MW; B2A470F9927326D2 CRC64;
MSSTKWTDEQ RQAIFTKNCN LLVAAGAGAG KTAVLVQRII EKILDKEEPI DIDKLLVVTF
TNAAAAEMRE RIGDAISKGL DEDPESKVLR KQLTLLNKSN IMTIHSFCLQ VIKNNFHTIE
IDPNFRICDE TEGILMKQEA IDELFDELYE IENEDFINLV ESYASRKDIR LQEVVLELHR
FAKSAPFPYT WLLNMAEGFN VGENFNFEET LWADMIMEDM KVLLHGFKNM LQQSIDVILN
SEGIDYYYEP FKMDLSFINS LLEKSSFKEF RGEIIAYDFP KLPLKRNKDA DKEAKERVKK
LRDRVKKRII ELRITLNSYE NEFTKKEFIF LYPSMKALSN LVILFDKKYE AKKRERDLID
FNDIEHLCLS ILTDKNSEGH IIPSDIALNY RKKFAEVLID EYQDSNLVQE VIMSMVSRVK
GYWSFYNGQL IFNEEEINLE EPQIGLDIPN RFMVGDVKQS IYRFRQAKPE IFLDKYNEYS
EEEGTKNRKV KLFKNFRSRE EVINGVNYLF KQIMSKTIGE LDYTEEEALK VGASYGEEVK
GEPIELCLMD KKYEISEEVL KEYNVDEEEA LDNIQLEGRL VAKKIQKLVG NNLEGGLKVF
DRKLGEYRNL QYRDIVILMR ATSNWAPVFV EELAKEGIPV FADTNSGYFD TAEIKTMISL
LQIIDNPLQD IPLLSVLRSP IASFTDDELI DIRMVNKNIT FYECMEIIYR LYKNEKLDSY
YSFYIEDENK INKIIKDMNE KLKNKICSFI EKLKLWREKS IHIDIDEFIW FLYVETGYYG
YAGALQAGEQ RQANLRILFQ RAKQYAKTSY KGLFNFINFI NKLKFSSGDM GSAKILGENE
NVVRIMSIHK SKGLEFPVVI LSGTGKNFNM MDLNKNILFH RDLGYGPDYV DTERRIAYPS
LVKNIIKNKI RLETLSEEMR ILYVALTRAR EKLIITGLIN NMDKTVEDWL NLSEDKNKVP
EYAVMSGKTY LDWIGPALIK HKDAVSFREE LKMTSELSNI VDDKSKWKIE LWNKRELLKE
KVEEDEVEIS EKIKETLMNL EESDYKEEIY KRLSFKYKYD NASSIPTKLS VSDVKKQFIL
DEKENTEELF KKLELRKPMF MEEKKKISPS ERGTIIHLFM QHLDLKKAEN EEDIKEQINR
LIEREFITYE QSKVISSYKI LKFCRGELGK RILNSNNVNK EMPFSIEIPA LEIYKELDKE
IYKDEKLIIQ GVIDCYFEEE DGLVLLDYKT DYVNDIEEIK NRYEIQIKYY EEALNRITGK
NVKDKYLYLF SVDNYIKID
