ID   ADDA_LIMRD              Reviewed;        1392 AA.
AC   A5VHK2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Lreu_0050;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82326.1; -; Genomic_DNA.
DR   RefSeq; WP_003669565.1; NZ_AZDD01000013.1.
DR   AlphaFoldDB; A5VHK2; -.
DR   SMR; A5VHK2; -.
DR   STRING; 557436.Lreu_0050; -.
DR   PRIDE; A5VHK2; -.
DR   EnsemblBacteria; ABQ82326; ABQ82326; Lreu_0050.
DR   GeneID; 66470128; -.
DR   KEGG; lre:Lreu_0050; -.
DR   PATRIC; fig|557436.17.peg.369; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001991; 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; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
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; 2.
DR   PANTHER; PTHR11070:SF48; PTHR11070:SF48; 2.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 2.
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..1392
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379286"
FT   DOMAIN          4..595
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          623..929
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   1392 AA;  159710 MW;  FF9599F8233A0394 CRC64;
     MAGFKPTPAQ SKAINDRGEN ILVSASAGSG KTAVLVNRTI ELIKEGQSID RMLLVTFTDA
     AAKNMRDKIR AALQKIVQDS ANPKDLRDRM SNQINRLAAA DISTIHAFCL KLIKRYYYLI
     DLDPQFRLLT DETERLLLQE DVWHEVSEEL YRNAEEKVSG KASFSELVLN FSSDRDDQGL
     DDLILRLYEI ANAQPDPEKW LQKLPDNYDL GSGSLLESNF YQQQLKPLVI EKLNQFIQDY
     RELVTRASDN GLDQAAEVIK SDEELMHQLL SSLGGITVSD VCQMMAQQKF GSFRGRPAAD
     DPRIDVFKDI QKQRNQLKKQ WEQMVSTYLG KQEAQEPIAK EELLTELTTF SDQFTDLLSK
     ATESQLDAKT VDSLQKDQQM MQELLDLLQP PTWNTIRDLF ANAKFARMGG KPKDDELAEE
     VYKSLGSART GIKKQFDQLV DRFFNYREDQ FRLISTHAQE LLRELSAVTI NFRRRYQQTK
     LNRHVLEFSD LEHYAYAILT PPDDQPNWQT LVKDLQNHYQ EIMIDEYQDT NRLQESILMK
     LTSPERKNLF MVGDVKQSIY RFREADPTLF LGKYQNYRQG SDGEAIVLGE NFRSMTNVTS
     FTNILFEQLM DREVGEIDYD EDAHLKYAAT YYEENQDNKV HPTEVLLYDA NALDPEKEDV
     EHEDDKLAGE FRMIGMRIKQ MVENQELIFH PEDGQMHPIQ YGDIVLLERT KAINNSLMEE
     FNKLNIPLTV HDVESYFQAT EVRVMMSLLK IIDNPQQDIP LVAVLRSPIV GLTNQELAFI
     RLQNRSVDYY AALQTFMSNY QRKALRHQSL LTSEQVNALY EKADHFLGLL RVFRQTAQQQ
     TLVDLIWQIY DQTGYLDYVG AMPGGHQRQA NLHALYQRAH SYEQSSFKGL YQFIRFIEKM
     QEHDKDLGVA PTQLTANTVN VMTIHGSKGL QFPVVFLIDA THGFNKGAAR ENAVVDAVAG
     VGIRYMDDQR VIYDTPQRQA VIEEIQRGER AEDLRVLYVA LTRAEQRLVI TGSFNEEMRT
     QSLAGSWQRW QKAYQSKNLL IGPQPRITAN SFMDWVGLAL ARYPEFNAQQ LSRGNVTLEE
     STLADTKVTG LAADPHFTAK TYTALDVSDG LAKIGQNASA NVTEKNNTVA TDASEQKIEQ
     ILRYRYPHLV ATKTTAYQSV TDVKRVFEDP DTRDMARWDY DQQQKVKTQG IYLNNNFDVP
     AFIQQTTHEP VATEIGTATH LVFQKLPLDE GLINVEFVDQ EIQKLVGEKL INPVVAARIN
     REGIVAFYQT AVGQKILKHP ADYHREVPFS MIMNGHELFK GVNVSDDERI LIHGIIDGYL
     RTDEGIILVD YKNDHLNKDY RDFDLARIKD RYRGQLELYK EALNLMEGIP VVQMGLYLLE
     LGEFVLFTKE GD