ID   ADDB_LIMRD              Reviewed;        1260 AA.
AC   A5VHK1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Lreu_0049;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82325.1; -; Genomic_DNA.
DR   RefSeq; WP_003669564.1; NZ_AZDD01000013.1.
DR   AlphaFoldDB; A5VHK1; -.
DR   SMR; A5VHK1; -.
DR   STRING; 557436.Lreu_0049; -.
DR   PRIDE; A5VHK1; -.
DR   EnsemblBacteria; ABQ82325; ABQ82325; Lreu_0049.
DR   KEGG; lre:Lreu_0049; -.
DR   PATRIC; fig|557436.17.peg.368; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000001991; 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; 2.
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..1260
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379376"
SQ   SEQUENCE   1260 AA;  143743 MW;  328506BF7AA5CCB8 CRC64;
     MGTLGFVLGT AAMDHQQVLI DQLVDQVKNT PADDTFYYLV PNHIKFETEI NVLAGLRDRQ
     GLSGSDRFAS SRVQVLSFSR LAWYLLRDTP AFQKQHLSKI GMAMLTSQVV QEQASDLRLY
     ASEVKQPGFI QKMTAQLEEL KNANITADDL TDIIYRVKSA NDPAANQAWL AKMYDVETIY
     HAYEARLRDR YIGNSELYRQ LVSYLQKSPE VAKMHFFIDR FAQFTANEQQ VVDALITNAA
     STTISLTLDR GYPDQNHPNP QELPPKNNLF YSSAMQFHRL WKFGQMHQKE VKVLQNVAFA
     TTPRVDAELQ QVDSYFKRYA SEPIGPGERE ELLDPQNIQF MTTTNRMTEL NNVATQIRQL
     VASGKYRYRD FLILSRHLDG YQTMIEPVFA AHNIPVFNDH ERLMDNHPLV TLLTTLLELP
     QRGYRTADII QLLKTWLLVP RTGTGDLMGL SDFQAAVFTT ENWCLKQAIE GKNAWTTNDP
     EKIKQLWQAP GTNLTDPKYE QSRLEKLNDQ LALVKDFVAN HLLPVFDQFK QAQTGQELAT
     ALYQFLAAMG VTDRLYAWQQ YQSTRDLDLA RQPQQVWTTF CQILQEYVEI LGQQELRDGT
     NEVLADFSEL LQAGFAAAQY SQIPATLDQV VVSETGIVQS ENRKVVFMIG STDDVMPEMQ
     ESDSLLTDQD KDILSAYLDE DFQYLPGTAI DQLIDEPFVH YTGFMNAKEQ LIFSAPQSDS
     DDKELSISPY MHDMARYFGQ PVREYPLATS KAGQDNAIDF VSAPLATINR LVEVSRQIRD
     EQGVGIDRQP VMPVGWQTVA ESLVKLAKQW QQSADAKVQA EGISLGQRLS LVAAGFHYQN
     KIDSLGNKLA QALYLRAAPD DERGRVLYAS ISQLQDFYIN QYEYFLKYGL RLQKRDELTL
     SNDRIGTFFH KAMETFVTTI RENNLSFADL AHKDNQMQRD QLIDHALVTA QENQPTLLRL
     INSSAQAQFQ YQQLTAIVKT MLITLCRQAE YTGSQPVKTE VQFGRIGNQQ PGNLGSLDYP
     LKDNHHIYLR GRIDRIDNLK QGNNNFLTVV DYKSSNHLFD LTSAYYGLSL QLLTYLNGLQ
     ANLTELETNN PRLAGALYLR LNNPTIKAAE LKKSSLDDLK LKEHQYKGIL LNDPQLLREL
     DKSLDKQAFL YPLKEYKNGK IKANKEALLV TPQQLDWLQN MNKELVINAG NQILSGDLKL
     NPYRLLTGSN RRTGLDYSDF LDVFQFDNML DQQNYRDLNP NLAKEAFDNV VQDDDEEDKK