ID   ADDA_LISMO              Reviewed;        1235 AA.
AC   Q8Y511;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=lmo2267;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
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; AL591982; CAD00345.1; -; Genomic_DNA.
DR   PIR; AC1358; AC1358.
DR   RefSeq; NP_465791.1; NC_003210.1.
DR   RefSeq; WP_010989936.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y511; -.
DR   SMR; Q8Y511; -.
DR   STRING; 169963.lmo2267; -.
DR   PaxDb; Q8Y511; -.
DR   EnsemblBacteria; CAD00345; CAD00345; CAD00345.
DR   GeneID; 985303; -.
DR   KEGG; lmo:lmo2267; -.
DR   PATRIC; fig|169963.11.peg.2319; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   PhylomeDB; Q8Y511; -.
DR   BioCyc; LMON169963:LMO2267-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..1235
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379296"
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;  142656 MW;  E0329AD6F07E4716 CRC64;
     MSLNIPPKPE ESLWTDDQWK AIQAKGNNVL VAAAAGSGKT AVLVTRIIEK LIDESANLNV
     DELLIVTFTN ASAAEMKFRI GKGLEEALGQ NPDSAHLKRQ VALLNYASIS TLHSFCLEII
     RKYYFEADID PSFRLIEPIE SSMIRDEVLE GLLEQEYGIE NNEAFFHLVE SFTGDRSDAE
     LHSLISKLYD FSRANPDPNA WLEAMVNFYN TEEITSITEL PYFPIIKEDI ELRVNQAKNY
     LLNAINYANE NNGPAPYLAT LENDLVQIQA LSELNWSSWT HLKTSIENID FKRIPTLKNK
     SDYDEVYVEE AKKFRDAAKK EMKNIATDWF SREEVNCLSD LEKMKPDIQT LSELVKKFSA
     NFFEEKQQRG VLDFNDLEHL ALKILLNDDK ASEVAQNYQK QFKEVLIDEY QDTNMVQETI
     LRLVTNPSEA QGNLFMVGDV KQSIYRFRLA EPTLFMTKYQ TFQQDGSGNG IRIDLSQNFR
     SRKEVLDATN FIFRQLMDKH IAEIDYDTAA ELTLGANFPE TNAMETELLL IDMKTEDTET
     EDELSPQELQ KNQVESRAIA MKIREMIDNK FPIYDKKLKQ NRPIQYRDII ILSRAMTSAP
     DMEEAMKVQD IPFYANNNSG YFETTEVATM IALMKVVDNP YQDIPLAAVL RSPIIGLNEE
     ELGQIRMAKK KGYFYDALLT YKDITVSETA NKISDFVQQL NNWRELSIRE NLTSLIWQIY
     QETNFYEFVG GLPGGKQRQA NLRALYDRAN QYEKTSFRGL FRFVRFVERL EIRGDDLGTA
     KTLGEKEDVV RMMTIHASKG LEFPVVIVSG LSRKFNMRDI YSKTLLDKDY GFASSYRDVE
     KMIVYPTIMQ QAIKQKKSRE MIAEEMRVLY VALTRAEEKL ILVATVPDFE KTSKNWLQVA
     KEKETILPAA TRAKAKCYLD WIGNATIRHP AFKELLCEEI IQTLATEMKL QIEIKTKEMF
     LTNELERAES DNWLENIKEH QPVPIQSPYK DEIQRYMEYE YQNEAATEIR AKQSVTELKR
     QFSLQDSWSD TTLLKEFQKV SLDRPKFLQK NKLSATEIGT AMHTLMQAVS LDYKPTKEDL
     EQLLHTMREK DILTDVQIKA INIKQILDFF ESPLGETMLQ KKDLVKREVP FSYLLPVSEL
     YEKVDLDERV LIQGVVDSMI EEEETITLID YKTDKIEGRY ADWNAAEKVM KERYHIQIKL
     YAEAIQAISG KKVAAAYLYF FDGQHICQIN TKEGL