ID   ADDB_LACH4              Reviewed;        1160 AA.
AC   A8YVK1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=lhv_1274;
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571;
RX   PubMed=17993529; DOI=10.1128/jb.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(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; CP000517; ABX27288.1; -; Genomic_DNA.
DR   RefSeq; WP_012211954.1; NC_010080.1.
DR   AlphaFoldDB; A8YVK1; -.
DR   SMR; A8YVK1; -.
DR   STRING; 405566.lhv_1274; -.
DR   EnsemblBacteria; ABX27288; ABX27288; lhv_1274.
DR   KEGG; lhe:lhv_1274; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000000790; 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   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; 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..1160
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379373"
SQ   SEQUENCE   1160 AA;  134065 MW;  EBF73F2424E3BD1E CRC64;
     MIKIITGRQT DPLQEKILAT AIENYQQHPE NETFIIVPNH IKFTTEVRAI NKLASSKKQT
     ETAVKNLHVL SFSRLAWFFL KDAEQGLPTQ LDDAASAMLL THIIEQKQDE LIIFEQSNSG
     MVRQLYNTIL QVYDGNLDLD NIDETNLDQE TKSKIHDLRI IYDAFIEEIA GKFSTKNEVQ
     VQLNDILAKN SELKNASFYF CDFSHFSLQE MLTIQILMRK AKNVTLAFKT RLGNINPKAE
     AGDYDYVIQQ TIRRLVSFLQ ERDMDYVASE FPIPSEPTPR EILNSLWTET VSKVDELKQV
     QLVKADSRYA EAYFVARTIY QQVALNNYRY RDFLILAPDL KEYETYLTPI LRQNNIPFFN
     DLQQEMKYHP LVVLIENLFN LRDLKENPFQ TQSMLAILKT HLLIPSWYKE EAEYIHDVDE
     LENFVLAHGI NHNLWKKHFA DFVSAEVIRL DKIDEEVAKI DRLRGYLVDK VTNLFTKLEQ
     EKDSQKALTI FFDFLTKNGI AERLEQWRDA ANNAGDLQQA QQPEQLWDLL IQLLKDYLAI
     NPEKFDLDEF FNMLISAFKE ATFSQIPSTL DAVNLSEMGM VQTSGYKQVF IIGATSGNLP
     SIEKKPGFLT TENLNQLQSS FESDAYLEDN QRLNNLDQNY QFGLSLALAQ DRVYISYPVL
     NASNEKLDPS IYYQRLQDYG APEFSQHDLP EKMQELLSFI TNPDASLGYL AYINSNTSDE
     AIDELLKITQ KYLPQKVKAV LDASDFDNQP EDIGEDLAAE LYGKNLYSSV SQLETFYENS
     YEYFLTYGLK LRRRLENEFD VIQAGNYFHE TFDRLVKRLN EQHIDLADLS SVELEQQLNQ
     VRDVIKDESK YAQLMNDPFN QYLFHCLDHT TSKVAQNWRK SLAETPLRAK YSELSFGLDQ
     KIKGISLDIP DLPGNHQVNL RGKIDRVDLA NFAEKDQVLA QVIDYKSSAK KFDLGMFYNG
     IALQMISYLD VLTNNNRFFA EEDKLSLLGA FYQTVTRQLE RLNSNKLIDS SLNLRENAID
     SKPKLMYTGL ISNNPEILLE AEPLLDGKSS QASQLYTGVG TKARGGFKLP ADRNFSEEEF
     QLLLEYDEYL IKEASRQILS GQIKLNPYRY GRSKNALTYS DFKDIFFFDA MLRHNQYHEI
     SNMSKKDLLV KIKEKLGKKD