ID   ADDA_CLOB8              Reviewed;        1245 AA.
AC   A6LPC4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Cbei_0014;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
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; CP000721; ABR32204.1; -; Genomic_DNA.
DR   RefSeq; WP_011967379.1; NC_009617.1.
DR   AlphaFoldDB; A6LPC4; -.
DR   SMR; A6LPC4; -.
DR   STRING; 290402.Cbei_0014; -.
DR   EnsemblBacteria; ABR32204; ABR32204; Cbei_0014.
DR   KEGG; cbe:Cbei_0014; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000000565; 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..1245
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379248"
FT   DOMAIN          4..477
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          517..815
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   1245 AA;  144478 MW;  28F44FDD93C4D845 CRC64;
     MGNTKWTDEQ LSAIETRNCN LLVAAAAGSG KTAVLVERII RIITNEENPV DIDKLLVVTF
     TNAAAAEMRE RIADAISKEL ENNPRSKNLQ RQLTLLNRAN ITTMHSFCLD VIKNNYHRID
     LDPSFRIGDQ TEGILIKSEV IEELFEDKYE EEDIGFTNLV EIFSSYKNDN NLKNLVLDLY
     NFTMSGPWPE KWLINSAEAF NIKQLDELDR TNWVRVLAQS VKIELDGYVK MLEKAIEVTS
     KTDGLEPYMD NLLMELSYIK KAYESTDNGL EAMFNSLSSV QFSRLKSIKK DKVSDELSQN
     TVKKIRDDVK KGISELLNNA YSVNPQQMLR NIQGSYPYIK KLIELVLEFS ARFSKRKRER
     NILDFNDLEH LCLKILSDYD DENNIIPSSI AMNFKEYFDE VLVDEYQDSN NVQETIINLV
     SRKNDDNPNV FMVGDVKQSI YRFRQAKPEL FIEKYNTYDS SNGVNRKIQL YKNFRSRREI
     IDGVNYIFKE VMSEVVGELE YTDEEALNLG ADFKENKFKD TIVGGPIEVN IIDKSHNETV
     VEDNEEQEEI NNVILEGRIV AKRIKELMSK SEDEQIFKVL DKESGEYRPL KYRDIVILLR
     ATKNWSEPLL DELSAEGIPV YADTGSGYFE SIEIRTIISL LKVVDNPMQD IPVISVMRSP
     IMGFSAEEIS DIRLVKKDNY FYENIKYISE EAYNSINESY SDVLIAKCKY FINSVDKWRN
     KSIYMAIDEF IWYLYMDTAY YGYVGAMPNG VLRQANLKIL FQRARQFEKT SFKGLFNFIN
     FINKLIKSSG DMGSAQVLGE NEDVVRIMSI HKSKGLEFPV VFLCGLGKNF NLMDLNKSIL
     YHDELGLGPD FIDIGKRFSI GTLAKESIKK KMKFETLSEE MRILYVACTR AKEKLIMTGT
     VGNLEKSAEK WLGSASLDYN RISPSEVLKG KSYLDWICMS LCQHRDGSVL SESFGTENLI
     LKDDNSRWKV SFWNKGDLID KTKTEVLEQG EGYELTIINN KPYDNYLYEE VDKILSYKYP
     FKASTTIKSN ISVSDLKRRH AEEDYDTEQL YREKVKVVPK FLQEKKGLTP SEKGTAVHFV
     MKKIDFNRVS STEEIKEQLH ELFEKEFLLS EELKVINPTK ILSFFRSDLG KKILDLNCRG
     EKIYREIPFY TEISSLEVDK TLDNIYKDEK IRLQGIIDCF FEYKGDIILI DYKTDYIMEG
     HEDEFKEKYR KQLDYYSDAI FKLTGKKVKY KYLYSFYLEK EIKII