ID   ADDB_LIGS1              Reviewed;        1193 AA.
AC   Q1WRR9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-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=LSL_1608;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABE00410.1; -; Genomic_DNA.
DR   RefSeq; WP_011476467.1; NC_007929.1.
DR   RefSeq; YP_536493.1; NC_007929.1.
DR   AlphaFoldDB; Q1WRR9; -.
DR   SMR; Q1WRR9; -.
DR   STRING; 362948.LSL_1608; -.
DR   EnsemblBacteria; ABE00410; ABE00410; LSL_1608.
DR   KEGG; lsl:LSL_1608; -.
DR   PATRIC; fig|362948.14.peg.1703; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000006559; 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; Reference proteome.
FT   CHAIN           1..1193
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379379"
SQ   SEQUENCE   1193 AA;  138141 MW;  639596BE76DD7C2E CRC64;
     MSLGFVLGDA TKNHRQVLLE QITNWQAEDP QAKIYYIVPN HNKFSAEVKV LDYLKSQQDN
     QDLFATSNVQ TFSFTRLAWY FMKDTATYQV NRITNAGLNM IVYRSLQEHS DELTIFKGEQ
     TQPGFIAQLV SQLIELQQSC ITYDDIERMK ENLSQQDTAD SAELEAKLHD IAIIYRDFMQ
     MTDSKYLKPA DILPSLTQYL QNEDLSNSYF IIEGFSQFTA QEQAIISVLL QRAKEVRIDL
     ILNRGVTDIE DLSDKQSLFY RSERTYYLLY QQARKAQVKI LNDVYPQELR VETPELQSLA
     KYWKESTDLK PINVEKIGDN HNLQVIKADT RMTEIKEIAT RIKQMVALKD YRYADFLLLT
     PDLNKYRNII EPIFNDYKVP IFVDLAKKMI DHPLVELLTA LFNVKARHYR YVDMMRLLKT
     ELLIPKTEYG YLGIKQFRQD LDLTENLILK FGFEGSQWLR KDDWVYYRFG SSDFGTQTDV
     QEKITKQVNV IRRYIKEILP PFFKQLDEAE NGKEAAQILM NFLIINGVPE QLINWRNKAL
     EQGDMVMADR PEQVWNLFCA LMDEYVDTLG DLSFKEEDFL NLLQTGFEGA TYRQVPSTLD
     QVIISETTAT QMNDRKVTFI FGATDLVMPN RIQNTMLLTD MDRELVQGTL DDEKYLSDTA
     EGRMAAEPFM NYLAFMTPKE RLYFSYPVAG VNEDGLRMSP YVNRIMKQFD LPLYEANGEP
     TLEDKKVLKF VATKRTALSN LIGVARQAKG QKQPLPVMWR YIYQKLQEDA TYRRLTRKLM
     AGIEYSNIPE RLKTEYAEKL YGKTLNTSVS KFEEFFKNHY AFFLKYGLKL KERDVFELSP
     ANTGEFYHMA LDKLLKTLKQ DKVSITDINK SQFDAYLQQV LGGMEQLPQF QILQSSNRMQ
     FILKQLGATV SQMGWALHNQ GQRTKMRPLE TEVLFGHVGT ENGLKALTYD LGNGHKVNVR
     GKIDRIDQMI IDNQRYLGIV DYKSSSHKFN YQDAYYGLAL QMLTYLNAML QNTDLLLDLN
     AGEEIKPAGA VYMHLQNPVI KQKDILKNPY SEVLLKQNKY DGLVLDDQEL LSNLDTSIEK
     AGNSIVYPVR KYADGHFGGI KNSGNVITFD NLMLLLKRNE ELIQEAAKLI FAGDVALNPV
     LWPDRRSALQ YSPYKAIMQF DELLGNQYYR LPKENTADIL QKLAQENSAE SEV