ID   ADDB_OENOB              Reviewed;        1161 AA.
AC   Q04GY8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01453};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01453};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01453};
DE   AltName: Full=ATP-dependent helicase/nuclease RexB {ECO:0000255|HAMAP-Rule:MF_01453};
GN   Name=rexB {ECO:0000255|HAMAP-Rule:MF_01453}; OrderedLocusNames=OEOE_0308;
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. This subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01453}.
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_01453};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01453};
CC   -!- SUBUNIT: Heterodimer of AddA and RexB. {ECO:0000255|HAMAP-
CC       Rule:MF_01453}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01453}.
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DR   EMBL; CP000411; ABJ56284.1; -; Genomic_DNA.
DR   RefSeq; WP_002823380.1; NC_008528.1.
DR   AlphaFoldDB; Q04GY8; -.
DR   SMR; Q04GY8; -.
DR   STRING; 203123.OEOE_0308; -.
DR   PRIDE; Q04GY8; -.
DR   EnsemblBacteria; ABJ56284; ABJ56284; OEOE_0308.
DR   KEGG; ooe:OEOE_0308; -.
DR   PATRIC; fig|203123.7.peg.320; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000774; Chromosome.
DR   GO; GO:0008409; F:5'-3' 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-EC.
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_01453; AddB_type2; 1.
DR   InterPro; IPR014141; DNA_helicase_suRexB.
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   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1161
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379385"
SQ   SEQUENCE   1161 AA;  133904 MW;  28FBEA239108ABD3 CRC64;
     MTLEIVRGFA DRDFRSELLE RIYEKYRIDP QARFFYIVPN HIKFSAEVDV LKKFGSLLGK
     NDQEAQAFSR LQVYSLSRLA WALTKERDQK TIISNQSVSI LVGQVLRELP IEKLNIFARS
     ARMPGFVANV AEQLLEIWRS GLTASEILPL HQFDDRLSEK IKVLALIETK ILPSLKDYSL
     PDDALRNFAT QISKIDLKNC NFYFEGFSGF TASELSLVKA LISADRKTQL GKKSEIVFSL
     TGEQQSDQYG EGNLFYRANQ LFKNEFSSAR VWIVSNIRPL SESQLNFEQS WRELETQGFT
     SQKRSFPQTK IVVSSDQEHE IDFVARSIRQ RLVDNPKLRA KDILVLAQRL DGYKNIIPKI
     FDRYDLPYFL DKDTRMSDHP LASLAENLLG SSNEFAYERI MKIFRTGLLS WQLEDNFQTA
     LDYLENYLLA NNPKEKNWRQ EEFQLIQISD EQDLNDDHKI DRQINALINR MRLFIIKILD
     DFQEKFAKVE NYHQAVKTLY NWLTDQQVDQ VLLNQANDGD DRGQQTWKLL LSTLDEVDQL
     IGDKKYSQKD FLQILKDGFA AASFSGIPAS LDQITVSESG IVQRNDFKAL YFIDASDASL
     PAQTNSSSLI DDFDRLQLID DFSKAQKPYY LQDTSRQEMT AENFRFYSSV LSATDSVTFS
     YSKLRLDGKQ NELSPYLRRL SLKNVSDLKI EKIPDLPQSQ ADLVDYLGTA NSSAAILSQT
     AQNFGEDFID GLTDLLIKRN PYFQRILQAL HYNNQPVTLR PELIKKLFGE DLRLSISQIE
     KYYSNPYEYF LQYGLRLKKR NQFTVDAALS GTYYHSIFEQ VINRLIGKRT DFHDLSDQEL
     KKLSQESAQN LIELPDFQIL QSDDHFRAVA RSLTDDVLLT LKLMHRANRL NNSRPIKTEA
     VFGKLSSDQQ REQSLSGLDF TLANGRKIYL RGKVDRIDQQ DLEHIFGTII DYKSNGKVFD
     FRDAYVGTEL QLLTYWLALS KNSSRIGINQ PGGAVFVQIR NKPADISQAL AHQIQLDQLI
     GDRAKQQVPD FQFHGILLDD QNYLANLQTV LAGQKAKYYN FGLTKKGQKT ARSDLVSKED
     LTVLLKHDEK KLVEAGNKII HGEFPLYPIK KNEQRSALTY SDYTEIMNFD RNFGNQYNNL
     TRYPKNKSEL ISKMREEEGE N