ID   ADDB_PEDPA              Reviewed;        1192 AA.
AC   Q03D70;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=PEPE_1833;
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. 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; CP000422; ABJ68852.1; -; Genomic_DNA.
DR   RefSeq; WP_011673919.1; NC_008525.1.
DR   AlphaFoldDB; Q03D70; -.
DR   SMR; Q03D70; -.
DR   STRING; 278197.PEPE_1833; -.
DR   PRIDE; Q03D70; -.
DR   EnsemblBacteria; ABJ68852; ABJ68852; PEPE_1833.
DR   GeneID; 33061292; -.
DR   KEGG; ppe:PEPE_1833; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000773; 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; -; 3.
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..1192
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379386"
SQ   SEQUENCE   1192 AA;  137874 MW;  547C47F993826C39 CRC64;
     MPLQFMYGPA SIDHLEGIAD RVIELQQQNV GQPVYYLVPN HIKFQSEIQL LQKLRQRRDV
     KSHIFAEKDV QILSISRLAW FFLRNSSIYQ YPRVTSSSSN MLLYRVILEH QDELTLFHNI
     DAQLGLVQKI ATQLAEFKQG NVGPDELGRV AENIAENSDA GMDIKAKLHD LGIIYSAYEE
     EIQSRFIDAS DITHTLTDEL SKMDLSGQSF IISGFSNFTA EEMSLIQALM KANGNVVIDL
     IMDKFPLYEK VSENSLFFEN EKIIFKFNAW AHENKVKSLE PVRLHRVRVN SDLLKLEKYW
     IESSEGQVGG SKQENNACVT IFQANSRYAE VEHVATLIRQ KMAKDPSLKF SDFSVLTRHL
     SDYSTIIKPI FDQMELPIFY DLQIAMKDHP LLELINALFD IRAHHFRYED VMRLLKTGLL
     FPETEDDPHG MDFFKSVHIT ENYVLKQGIY GDRWLQKKDW KYSRFNDIDE EKQTDEEIEI
     NQRINTVKNY VAETVVPFFN QLSTATTGVE AAKALYDFLI KNGIDQCLLA WRDQWIEEGR
     LAKAAEPEQT WETFIQMLDE FVDILGDQPF DPDNFMGLLN AGFEGATYSQ IPSTLDQILV
     SESGMVQMVD RKIVFIIGAT DRVMPEQIQD NDFLNQDGKN QIDPFLDDDQ FLRISNDRQM
     RQEPYLNYLT FMIGSDELIF SYPKSGNDGV ELKISPYVER IGKHFGIIAQ SLPSRPTTEP
     VRLDPPFIEL FIGSNRSTLS HLIQYARAMH EAKSEADPRW NLIYTILRQS TLGSLTDQLL
     SSLEYKNIPE KLKPEIVEGL YGDTIYASVS KLEEFYRNEY SYFLKYGLKL QERETSDLSP
     ADTGQYFHAA MDKLIKMITT ENLNFNEVNQ EQIEQIAKRL VQQMEQDQQF DQFNGTYRMG
     FLRKQLDRTV QAMVEAIFKQ LARTRMRPIA SEQLFGQIGS QSGLPALNFK VGEGKEINVR
     GKIDRIDKIE IGDKDYLGIV DYKSSNRKFD FTDAYYGLAM QMLMYLDVVQ RNKEKIDPAT
     KAEISSALYM IFQYPLLKSK EWKGSDANQL NQSIFKKFSL NGFLLKDEEL IKEIDKTIED
     TRKSDVFPIA FTTKGTLTKV SENSILSEDE LQNLIKHAEL KVREAGEKIF KGELDMNPVQ
     WPNRRTVMEY SPYKDVMQFD AMLPENNYRI IEKLDKDKVL EQIREEQEKN GR