ID   ADDB_LEUCK              Reviewed;        1171 AA.
AC   B1MZM3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=LCK_01148;
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20;
RX   PubMed=18281406; DOI=10.1128/jb.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82975.1; -; Genomic_DNA.
DR   RefSeq; WP_004908913.1; NC_010471.1.
DR   AlphaFoldDB; B1MZM3; -.
DR   SMR; B1MZM3; -.
DR   STRING; 349519.LCK_01148; -.
DR   EnsemblBacteria; ACA82975; ACA82975; LCK_01148.
DR   KEGG; lci:LCK_01148; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000002166; 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.
FT   CHAIN           1..1171
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379383"
SQ   SEQUENCE   1171 AA;  132448 MW;  5568E84954912EDA CRC64;
     MSLTVYMNHG QIDMRHALLS HAHEALNQDN NLTVYYIVPN HVKFDSEVDV LRRFARLTGQ
     NPDTSLYAQS RLQVYSLSRL TWALLKDMAT MQPNVIQGTG LFIMVSDILR DYAAQLPIFA
     RMQSKAGFVT TLVAQLVELR ASRISPEDLL TILNQESDDD TFLRQTLSGK LRDLAIVADA
     LDKKMGHTYI TQQEVLSFFA TQLATTQLKN VAFYFDGFNG FTSPETQVMI ELMARYPVTV
     ALLGDVEKLG SQQPGDLFYK PMTTAQRLAQ FTKIANQQVV WQVPTQARCL DESIISVMSA
     WEKLGEYRQF NSENKKTNLA AFVAENTMVE IQEVARRIRQ LLVAQPDLRL RDILILARDL
     TPYTGHIPEV MQQFDLPYFL DTDQKMTNHP LVELLLNLLR PAKERFQYQQ VMAILKTGLL
     RPYTDGSLVP EGDFFDIVSY LDNYLYANQP FERTWRDLDH PFTLFTVSED EDDEDARVVL
     DDKTVNRRIE TLRRFVIDAF DSLQQQLNQA QTMRQAATLI ILWLEKYHVT EAILSQRDTL
     LAAGELSRSR EGEEVWEMMT QTLDDIVAID GDERFELEKF KAILVAGFEG ATFSGIPNNL
     DQLTISEAGI VQSNDYQYLF FIGGTRNNLP AQLKSRALIN DAERLIVQPA LQENSTPKYL
     QNTAQQQMAE ENLLFYGALT AATKNIVLSY PALDAGGQIS DMSPFFKRLV DAFNITVNKV
     TATPATSQAL LKYYVGSVRS TLGELVKIAA SQQQTSAYQA LRNTINQSEP ERLERVLSAP
     NYKNQTETLK PELVQALFGE TLNMSISQLE SYYNNPLAYF LQYGLALKER LTNRLNVAQT
     GTLYHAVFEG VVQQLIIQQL SLRDISQKAL QQLVADNMAE ITAQPAYQML QETGKMRATQ
     HYLAKVSEIL AVNMQRAARV NHAQPKAVER LFGFPNRQSL PALVVSTPQA TVHLRGKIDR
     LDSQDPSQVY GTIIDYKSNG KHFDWGQAYD GRQMQLLTYW QAAQLSAEQL GIEAIGGAFF
     AKIAPEKLTI KDFKGDVRAM LRGEIKPEQF KYRGLFISEP AYIDSLETLA EGEGSQFYQL
     KKKANGELYA NSDVISPEDF ELLLKRNLDN IQRASAAILS GDFPLSPAEG SLQFTPFTDV
     LRFDRALGDQ YKNNTPKNKS DILKLLKADE E