ID   ADDA_LISMF              Reviewed;        1235 AA.
AC   Q71X99;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
GN   OrderedLocusNames=LMOf2365_2300;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT05066.1; -; Genomic_DNA.
DR   RefSeq; WP_010959028.1; NC_002973.6.
DR   AlphaFoldDB; Q71X99; -.
DR   SMR; Q71X99; -.
DR   KEGG; lmf:LMOf2365_2300; -.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
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; ISS:JCVI.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004527; F:exonuclease activity; ISS:JCVI.
DR   GO; GO:0006259; P:DNA metabolic process; ISS:JCVI.
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_0000379298"
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;  143004 MW;  964A9809977724F0 CRC64;
     MGLNIPPKPE SSLWTDDQWK AIQAEGNNVL VAAAAGSGKT AVLVTRIIEK LINESANLNV
     DELLIVTFTN ASAAEMKFRI GKGLEEALAQ NPDSTHLKRQ VALLNYASIS TLHSFCLEII
     RKYYFDADID PNFRLIEPIE SSMIRDEVLE NLLEQEYSIE NNEPFFHLVE SFTGDRSDAE
     LHALISKLYD FSRANPDPNI WLEEMVDFYN TEETTSITEL PYFPIIKEDI ELRVNQAKNY
     LLNAIDYANE NNGPVPYLAT LENDLAQIEA ITELSWNSWG QLKKAIESID FKRIPTLKNK
     SDYDEEYVEE AKKFRDAAKK EIKNIATDWF SREEINYLSD LEKMKPDIKT LSRLVKKFAE
     NFFEEKQQRG VLDFNDLEHL ALKILLKDNE ASEVAKNYQK QFKEVLIDEY QDTNMVQETI
     LRLVTNSGEE QGNLFMVGDV KQSIYRFRLA EPTLFMTKYQ TYQQDGNGSG IRIDLSQNFR
     SRKEVLDATN FIFHQLMDKH IAEIDYDAAA ELTLGASFPE TTDMATELLL IDMKSVESET
     EDELSPQELQ KNQVESRAIA MKIKEMIDNK FPIFDKKMKQ NRPIQYRDIV ILARAMTSAP
     DMEEAMKVQD IPFYANNNSG YFETTEVATM IALMKVIDNP YQDIPLAAVL RSPIIGLNEE
     ELGQVRMAKK NGYFYDALLT YKDTTVSETA DKMSDFIQQL NNWRELSIRE NLTSLIWQIY
     QETNFYEFVG GLPGGKQRQA NLRALYDRAN QYEKTSFRGL FRFVRFVERL EVRGDDLGTA
     KTLGEKEDVV RMMTIHASKG LEFPVVIVSG LSRKFNMRDI YSKTLLDKDY GFASNYRDIE
     KMIVYPTIMQ QAMKQKKSRE MIAEEMRVLY VALTRAEEKL ILTATVPDFE KTSKNWLQVA
     KEKETILPAS TRAKAKCYLD WIGNATIRHP NFKELLCEEM IQTLPTDMKL QIEIKTKEMF
     LTNELEKTET VNWLENIKEH QPIPVKSPYK DEIQRYMNYE YQNEEATEIR AKQSVTELKR
     QFSLQDSWSD TTLLKEFQKV SLDRPKFLQQ NKLSATEIGT AMHTLMQAVS LEHQPTKEDL
     EQLLQTMREK DILTEAQLKA INIKQVLGFF ESQLGKTMLQ KKDLVKREVP FSYLLPVSEL
     YEKVDIDERV LIQGVVDSMI EEEETITLID YKTDKIEGRY SNWEAAEKIM KERYHIQIKL
     YAKAIQAISG KKVDAAYLYF FDGQHICQIN TKEGF