ADDA_CLOBL
ID ADDA_CLOBL Reviewed; 1279 AA.
AC A7GAJ8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=CLI_0522;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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; CP000728; ABS39663.1; -; Genomic_DNA.
DR RefSeq; WP_011987449.1; NC_009699.1.
DR AlphaFoldDB; A7GAJ8; -.
DR SMR; A7GAJ8; -.
DR EnsemblBacteria; ABS39663; ABS39663; CLI_0522.
DR KEGG; cbf:CLI_0522; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000002410; 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_0000379253"
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; 150195 MW; 4F9B5E60B86D472A CRC64;
MSGTKWTDEQ RQAIFTKNCN LLVVAGAGAG KTAVLVQRII EKILDKEEPI DIDKLLVVTF
TNAAAAEMRE RIGDAISKGL DEDPESKVLR KQLTLLNKSN IMTIHSFCLQ VIKNNFHTME
IDPNFRICDE TEGILMKQEA IDELFDELYE IENEDFINLV ESYASRKDTR LQEVVLELHR
FAKSAPFPYT WLLNMAEGFN VGENFNFEET LWADMIMEDM KVLLHGFKNM LQQSIDVILN
SEGIDYYYEP FKMDLSFINS LLEKSSFKEF RGEIIAYDFP KLPLKRNKDA DKEAKERVKK
LRDKVKKKIV ELKNILDSYE NEFIKKEFIF LYPSMKALSN LVILFDKKYE AKKRERDLID
FNDIEHLCLS ILTDKNSDGH IIPSDIALNY RKKFAEVLID EYQDSNLVQE VIMSMVSRVK
GYWSFYNGQL IFNEEEINLE EPQIGLDIPN RFMVGDVKQS IYRFRQAKPE IFLDKYNEYN
EEEDRKNRKV KLFKNFRSRE EVINGVNYLF KQIMSKTIGE LDYTEEEALK VGASYGEEVK
GEPIELCLMD KKYEISEEVL KEYNVDEEEA LDNIQLEGRL VAKKIQKLVG NNLEGGLKVF
DKKLGEYRNL QYRDIVILMR ATSNWAPVFV EELAKEGIPV FADTNSGYFD TAEIKTMISL
LQIIDNPLQD IPLLSVLRSP IASFTDDELI DIRMINKNIT FYECMEIIYR LYKNEKLDSY
YSFYIEDENK INKIIKDMNE KLKNKICSFI EKLKLWREKS IHIDIDEFIW FLYVETGYYG
YAGALQAGEQ RQANLRILFQ RAKQYAKTSY KGLFNFINFI NKLKFSSGDM GSAKILGENE
NVVRIMSIHK SKGLEFPVVI LSGTGKNFNM TDLNKNILFH RDLGYGPDYV DTERRIAYPS
LVKNIIKNKI RLETLSEEMR ILYVALTRAR EKLIITGLIN NMDKTVEDWL NLSEDKNKVP
EYAVMSGKTY LDWIGPALIK HKDAVSFREE LKMTSELSNI VDDKSKWKIE LWNKRELLKE
KVEEDEVEIS EKIKETLMNL EESNYKEEIY KRLSFKYKYD NASSIPTKLS VSDVKKQFIL
DEKENTEELF KKLELRKPMF MEEKKKISPS ERGTIIHLFM QHLDLKKAES EEDIKEQINR
LIEREFITYE QSKVISPYKI LKFCRGELGK RILNSNNVNK EMPFSIEIPA LEIYKELDKE
IYKDEKLIIQ GVIDCYFEEE DGLVLLDYKT DYVNDIEEIK NRYEIQIKYY EEALNRITGK
NVKDKYLYLF SVDNYIKID
