ID   ADDA_PEDPA              Reviewed;        1235 AA.
AC   Q03D71;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=PEPE_1832;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
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; CP000422; ABJ68851.1; -; Genomic_DNA.
DR   RefSeq; WP_011673918.1; NC_008525.1.
DR   AlphaFoldDB; Q03D71; -.
DR   SMR; Q03D71; -.
DR   STRING; 278197.PEPE_1832; -.
DR   PRIDE; Q03D71; -.
DR   EnsemblBacteria; ABJ68851; ABJ68851; PEPE_1832.
DR   GeneID; 33062088; -.
DR   KEGG; ppe:PEPE_1832; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000000773; 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; 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; 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_0000379305"
FT   DOMAIN          4..470
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          501..795
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   1235 AA;  141725 MW;  C00705D32ED026BC CRC64;
     MADREYTLSQ KQAINSSGHN ILVSASAGSG KTSVLVERVI QKIINGEDVD RLLVVTFTEA
     AASEMKERIR AAIVKKINEV SDIELQNHFS MQLNKLNNAN ISTLHAFCMS IIRNYYYIID
     LDPTFRIMDP TESELLKESV WADLREELYE RDEDGKFALL TRNFSSDRSD EGLQDLILEL
     FEFSNANPDP QAWLQQIAKN YEVPSDNVMD MEFIQQLLTE VKTKLMRIYR KDLDLTEQAI
     NGGEPLKNAA EKFQNEVDDL KTIIDSLNGS WDDVQQAVSK MKFAQLPRGK KEEVQEFNAY
     AKSIRNDFKD EFNTIADKYF KLSSEQMIAV FKDAHDLMMK LIEVQNQFAE RFLQEKLTRR
     SLDFSDLEHF ALQIVLDDSE EGQAIRRDFQ QKFNEVIVDE YQDINPLQET ILTSVASPDP
     GNMFMVGDVK QSIYAFRMAD PSLFISKNNQ FKDEEQADER IILAENFRSM RNVDDFTNLI
     FNQVMDTEVG EIEYDDDAQL QFGAKYYPDE VQNNTEVMIY DDSQTDINDK EATPIISNKN
     DGQLQMIAQR IQKLFADHTQ IYDKKEQKMR DLEYSDIALL HSTGSNNLEI VDTFKKYGIP
     IQVNNAQDYF QTTEVSIMMA LLKIIDNPYQ DIPLAAVLRS PMVGLKENEL AFLRIGKKNG
     HYFEALLYFL NEAKLDSNNE FQMQLKTKIT HFLEQLDHFS KLARQSTLVD LLWAIYDETG
     YLDYVGGMPD GPQRQNNLHA LYDRAKGYEE SSFKGLFQFV RFVEKMRDKN KDLAENPVVT
     DVKAVKLMTI HGSKGLEFPI VFLIDAEHGF NTMDEKGRYV LDRDAGMGIT LKDFIHRLEI
     DTVQKNWIIS IKKQKALAEK LRVLYVALTR AEQKLIITGA VNSADDTLNK WAEAVDTDET
     LIPAEARSKV SNFLDWIGMA IMRVPSVVEK YADYNTRKLQ GTLIPDVELK IINSSELMDQ
     QGLTALKSAQ IPELQQLNAF DDIADVDKFK QIMNFKYHDE AATTTTAYQS VSEIKRVFDD
     PDKFELNFSE VDADQHIKPQ NRFVTESLMA PRFMNEATKP KAAEIGTATH LILQQLDLNQ
     PINETIIKDK IGELVMNRVL DEQVANRIRI STILDFFDSD LGQLMINHPE NVHREEAFSL
     LLPAKGLFPK VKGDDDVLIH GIIDAYFEME DRVILLDYKT DFVLPGSVEQ GIEKVINRYQ
     GQVNLYAQAL GSILKRPVNE KYLYLLSIGR LVEIQ