ADDA_CLOB6
ID ADDA_CLOB6 Reviewed; 1279 AA.
AC C3L047;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=CLJ_B0507;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
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; CP001083; ACQ53258.1; -; Genomic_DNA.
DR RefSeq; WP_003359648.1; NC_012658.1.
DR AlphaFoldDB; C3L047; -.
DR SMR; C3L047; -.
DR PRIDE; C3L047; -.
DR EnsemblBacteria; ACQ53258; ACQ53258; CLJ_B0507.
DR KEGG; cbi:CLJ_B0507; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002333; 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_1000215324"
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; 150122 MW; BAB23CA7CA6A54B4 CRC64;
MSSTKWTDEQ RQAIFTKNCN LLVAAGAGAG KTAVLVQRII EKILDKEEPI DIDKLLVVTF
TNAAAAEMRE RIGDAISKGL DEDPESKVLR KQLTLLNKSN IMTIHSFCLQ VIKNNFHTIE
IDPNFRICDE TEGILMKQEA IDELFDELYE IENEDFINLV ESYASRKDIR LQGVVLELHR
FAKSAPFSYD WLLNMAEEFN VGEEFNFEET PWADMIMEDM KVLLHGFKNM LQKSIDVILN
SEGIEYYYEP FKMDLNFINS LLEKLSFKEF RGEIIAYDFP KLPLKRNKDA DKEAKERVKK
LRDKVKKRII ELRITLNSYE NEFTKKEFIF LYPSMKALSN LVILFDKKYE AKKRERDLID
FNDIEHLCLS ILTDKDSKGH IIPSDIALDY RKKFAEVLID EYQDSNLVQE VIMSMVSRVK
GYWSFYNGQL MFNEEEINLE EPHIGLDIPN RFMVGDVKQS IYRFRQAKPE IFLDKYNEYS
EEEGIKNRKV KLFKNFRSRE EVINGVNYLF KQIMSKTIGE LDYTEEEALK VGASYGEEVK
GEPIELCLMD KKYEISEEVL KEYNVDEEEA LDNIQLEGRL VAKKIQKLVG NNLEGGLKVF
DKKLGEYRNL QYRDIVILMR ATSNWAPVFV EELAKEGIPV FADTNSGYFD TAEIKTMISL
LQIIDNPLQD IPLLSVLRSP IASFNDDELI DIRMVNKNIA FYECMEIIYR LYKNEKLDSY
YSFYIKDENK INKIIKDMNE KLKNKICSFI EKLKLWREKS INIDIDEFIW FLYMETGYYG
YAGALQAGEQ RQANLRILFQ RAKQYAKTSY KGLFNFINFI NKLKFSSGDM GSAKILGENE
NVIRIMSIHK SKGLEFPVVI LSGTGKNFNM TDLNKNILFH RDLGYGPDYV DTERRIAYPS
LVKNIIKNKI RLETLSEEMR ILYVALTRAR EKLIITGLIN NMDKAVESWL NLSDDKNKVP
EYAVMNGKTY LDWIGPAIIK HKDAVSFREE LKMSSELSNI VDDKSKWKIE LWNKKELLKE
KVEEDEVEIS EKIKETLMNL GESNYKEEIY KRLSFKYKYD NASSIPTKLS VSDVKKQFIL
DEKENTEELF KKVELRKPMF MGEKKKISPS ERGTIIHLFM QHLDLKKAEN KEDIKEQINR
LIEREFITYE QSKVINPYKI LKFCRSELGK RMINSNNINR EMPFSIEIPA VEIYRELDKN
IYKDEKLIIQ GIIDCYFEEE EGLVLLDYKT DYVNDIEEIK NRYEIQIKYY EEALNRITGK
TVKDKYLYLF SVDNYIKID
