ID   ADDB_LIMF3              Reviewed;        1245 AA.
AC   B2GEY3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=LAF_0036;
OS   Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS   fermentum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(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; AP008937; BAG26372.1; -; Genomic_DNA.
DR   RefSeq; WP_012390673.1; NC_010610.1.
DR   AlphaFoldDB; B2GEY3; -.
DR   SMR; B2GEY3; -.
DR   PRIDE; B2GEY3; -.
DR   EnsemblBacteria; BAG26372; BAG26372; LAF_0036.
DR   GeneID; 61200774; -.
DR   KEGG; lfe:LAF_0036; -.
DR   PATRIC; fig|334390.5.peg.35; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000001697; 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..1245
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379371"
FT   REGION          737..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1245 AA;  139712 MW;  D5F1763E5632E992 CRC64;
     MATLQFVLGS ASFDHQQVML DRLAAQYQQA PNDTYLYLVP NHVKFTTEVA VLKGLKKRLK
     QTGNYAQANV AVLSFSRLGW FLCKDDPDYQ KPRLSNVGMA MVVAKIIREL KAESPDLLKM
     FRGESERQGF ATEVTKQLVE LQNANIQPAD LAPDQETGII KRALASQAGG GRASQSTVFT
     DKMTVLYEIY RRFEAAVTTH VTAPDRSAML LNHLEAADLS TTHVYLDRFA GEFSAQEQLI
     VDALIQRAAD TTVSLILDRD YRGRELPSQN NLYYRSAKQY QDLLNLATQQ VGVDVLDPIV
     LNQPNQRRVS DALVGVEEWM EADARFALPD RLPAPTDQVG FFTAPTRVAE LNRVATKIRQ
     LVATGQYRYR DFLVVTRHLD GYQTMLEPIF SRHQIPVFND NQRPMATSPL ATFTAALFKV
     LKDYYQEADV MELLKTGLLV PETPEELQQE GRAKRNPNTF MTAVYRTENY CLKFGKGGRS
     WFDERPWRLE GEQPESDALK RQNAQINWVK NYIKDELAPA LADLQTATTG RELATKFYQF
     LLDQGVRHQL YSWAHQAQES GQLTQLRDVQ QIWQTFGTLL DEYVTILGDQ VAPTEQPGQL
     VAEFADLMNA GFNAGRYAQI PSTLDQVLVS ESGMIQDNQR KVLFIMGATD DVMPEVKASE
     GLLSDPDREL LKRGLNDDQF LPISGTDQIN NEPFLNYLSM LSVTERLYMS APLMSSDDSE
     LTLSPYLKGL ARHFNQWDDQ NNAPTTDLPD RPNPRASEDD VWSFVAAPAV TMGNLIEVER
     LSKDTGRKLT SAWRDVARAL TRYDEGLTGR LNDIRDGQYA KNEAVPLQPE LAARLYTTNR
     QGQVTNQLTA SISQLEKFYQ NPYDYFLRYG LHLKKRDELE VSSDKSGTLN HDALAFFVQS
     VIDEPDLQLA DLVKEEHQGR QAELIDQAFE QAMNQQEELR ELAANNSRVN LQLQVAKQLI
     TTMAKTLCLQ ATQTDAQPVA VEKAFGQADW TGESQAAELP ALTFDLTGAG LGEGAKVSLR
     GRIDRLDELK LGEQTYQLVV DYKSYNKAFD LVDAYAGQAL QMLAYLNALQ AANPGKQLLG
     SLYLRLYVPT VDAGKEGTAE ELKEHLYQGI TINDDAVLAA LDHGLGEKGA TLLSIKKKSK
     KDTSRFKVSA DDQFSAKAGS NLVSPTDLKR LMDHNAELIK EAAVQILQGQ NEIRPYRRQV
     GTTAETGLAF SDFLDVSRFD QALDDYKEIE LTDADVEAKF EQEEE