ID   ADDA_OENOB              Reviewed;        1186 AA.
AC   Q04GY7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=OEOE_0309;
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000411; ABJ56285.1; -; Genomic_DNA.
DR   RefSeq; WP_011677413.1; NC_008528.1.
DR   AlphaFoldDB; Q04GY7; -.
DR   SMR; Q04GY7; -.
DR   STRING; 203123.OEOE_0309; -.
DR   PRIDE; Q04GY7; -.
DR   DNASU; 4416235; -.
DR   EnsemblBacteria; ABJ56285; ABJ56285; OEOE_0309.
DR   KEGG; ooe:OEOE_0309; -.
DR   PATRIC; fig|203123.7.peg.321; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000000774; 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; Reference proteome.
FT   CHAIN           1..1186
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379304"
FT   DOMAIN          2..460
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          487..771
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1186 AA;  136211 MW;  BAB94E7523A83738 CRC64;
     MNFSKNQRAV IAHIPDHNLL VAASAGSGKT TVLIEHVYQQ LLSGKSIDRF LISTFTDAAA
     LEMKNRLEKR IRAGITEEEG QLKRHLQEQL LLLNSAAIGT LDSFSLRIIE RYYSVIGLDP
     RYRMLADQTE KNLLVKDVLD DTFDEMYHDE KFLRLLNNFS SASHDQDLKN LVIKLNTMAE
     TRANPDFWLD SIAENYRLSG GLTKGSFWKE LLQPQIFNRA SAALYQLLSA KKGVEDLEDY
     HSYIAYLADA VGLVRGFIEV CSQNNWQQMS DYFVNNSWPK SARKSGKNEQ EADYFDNWIK
     PWIKEAKDSY RSIESDFLFL NESQWLDISE KSLGVVEELI RLTKVFRKKF ALKKRELSLL
     DFSDGEQFAY QILQNQTVRE EIQSLFDEVL VDEYQDINDL QENILTDVSN GSNFFMVGDL
     KQSIYGFRQA DPVNFSNKYI QYKEGNGGEL IELSENYRSQ HNVADFTNAV FRKLMDRKLG
     GIDYRGDVEL KAANRDYPKN LKNVADISIF DIDEESNEDE DFNSRQAQIE IIAAKIQALV
     GQSEIYDRQS GKMRPLVYRD ITILERSHSW ENDIQTIFKK YHIPINVAAG NFLQEFEVSI
     VLSFLKIIDN PHQDIPLVAV LRSPIYGLDE NQLAEIRTAD MKHDYFSALQ AYAKTGQDLD
     LQKKMAAFLV QLENYREIAA DNQIVDLIWQ IYNDTNWPEY VAGMVGGSQR QANLHALYQY
     AQQLSDNHFV GLFSFIRYVE QLMDSVEDFA QAPVDMGQEA VSVMTIHAAK GLEFPIVFLL
     NLDKQIDNRD SNGAMVVDFD NGIGIDFVHP TSQVKIPTIQ KIAVAEKIKE KNWAEEMRLL
     YVALTRAEQR LYLVGSSKRM SDLIHNWGTP VSIGKKVIAF QDRMRAKSYQ SWIGMSLANS
     GYIKLDKVEG NYSKKDLTFK IESYNAQTIP KIVENKAKIK QNEQEETGID LARSKKILDY
     NYPYKIESEL AAYHNVSELK RVFEDPDSLL MPEMNSDRQP QITELPEPKF IGGNDQEQVS
     STDKGTATHL ILEKIDWKKE IDKDYLQQLI KENIPDQKTR QSIELDRIIW FANSEFGTEI
     KKSASTLKRE QTFAMLIPAK QIYQQVETSD PVLVHGIIDG YFISDGLITL FDYKTDRFGK
     DYVSKLKERY SGQLNLYAAA LSSIYPNLKV ERKVVVGLQG KRLIYL