ID   ADDA_LISIN              Reviewed;        1235 AA.
AC   Q929A9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=lin2368;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL596172; CAC97595.1; -; Genomic_DNA.
DR   PIR; AC1728; AC1728.
DR   RefSeq; WP_010991144.1; NC_003212.1.
DR   AlphaFoldDB; Q929A9; -.
DR   SMR; Q929A9; -.
DR   STRING; 272626.lin2368; -.
DR   PRIDE; Q929A9; -.
DR   DNASU; 1131127; -.
DR   EnsemblBacteria; CAC97595; CAC97595; CAC97595.
DR   KEGG; lin:lin2368; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000002513; 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..1235
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379295"
FT   DOMAIN          12..482
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          509..800
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1235 AA;  142869 MW;  7560961BD9EAE249 CRC64;
     MRLNIPTKPE DALWTDDQWK AIQANGNNIL VAAAAGSGKT AVLVTRIIEK LINETENLNV
     DELLIVTFTN VSAAEMKYRI GKSLEEALVQ NPESVHLKKQ VALLNYASIS TLHSFCLEII
     RKHYFEADID PNFRLIEPIE SSMIRDEVLE DLLEKEYSIE NNEGFFHLVE SFTGDRSDAE
     LHTLISKLYD FSRANPNPDL WLEQMVSFYD TQAITSITEL PYFPIIKEDI QLRINQAKSY
     LLTAIDYANE NNGPAPYLST LENDLAQINT LSSISWDNWQ DVKFGFESID FKRIPALKNK
     ADFDEEYVEE AKKFRDAAKK EVKNVLIDWF SREEENYLSD LEKMKPDIKT LSELVKKFAE
     NFFEEKQQRG VLDFNDLEHL ALKILLKNGA PSDVANSYKK QFKEVLIDEY QDTNMVQETI
     LLLVTNSNDT KGNLFMVGDV KQSIYRFRLA EPTLFMAKYQ EYQQDGEGSG IRIDLSQNFR
     SRKEVLDATN FIFHQLMDKH IAEIDYDEAA ELTLGASFPE ANNMATELLL IDMKSEEKES
     EDELSPQELQ KNQVESRAIA TKIREMIDNK FPIYDKKLQQ NRPIQYRDIV ILARAMTSAP
     DMEEAMKIKD IPFYANNNSG YFETTEVATM IALMKVIDNP YQDISLAAVL RSPIIGLNEE
     ELGQIRMAKK KGYFFDAMLA YKDITVSDAA NKISRFITQL NNWRELSIRE NLTALIWQIY
     QETNFYEFVG GLPGGKQRQA NLRALYDRAN QYEKTSFRGL FRFVRFVERL EVRGDDLGTA
     KTLGEKEDVV RMMTIHASKG LEFPVVIVSG LSRKFNMRDI YSKTLLDKDY GFASNYRDIE
     KMIVYPTIMQ QAIKQKKYRE MIAEEMRVLY VALTRAEEKL ILTATVPDFE KTSKNWLQVS
     NQQETILPAA IRAKAKCYLD WIGNATIRHS HFKELLCEEK IKTLPTDMKL QVEIKTKEMF
     LTDDLEKEKS DNWMENVKAH KQVPVKSPYK DEIERFMHYQ YKDEEATGIR AKQSVTELKR
     QFSLQDSWSD TSILKEFQKV SLDRPKFLQQ NKLSATEIGT AMHTLMQAVP LDDKPTEKDL
     VSLLQLMREK DILTEAQIKA INVNQIIAFF ESALGKTVLQ KKDKVKREVP FSYLLPAAKL
     YNQTNLDEHV LIQGVVDSMI EEEDSIILID YKTDKIEGRY DNWEAAEKVM KERYQIQIKL
     YAEAIQAISR KKVSHAYLYF FDGQHICQIN IEEGI