ID   ADDB_LATSS              Reviewed;        1186 AA.
AC   Q38X70;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=LCA_0909;
OS   Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS   subsp. sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA   Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI55211.1; -; Genomic_DNA.
DR   RefSeq; WP_011374611.1; NC_007576.1.
DR   AlphaFoldDB; Q38X70; -.
DR   SMR; Q38X70; -.
DR   STRING; 314315.LCA_0909; -.
DR   EnsemblBacteria; CAI55211; CAI55211; LCA_0909.
DR   KEGG; lsa:LCA_0909; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   BioCyc; LSAK314315:LCA_RS04565-MON; -.
DR   Proteomes; UP000002707; 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; 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..1186
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379378"
SQ   SEQUENCE   1186 AA;  136081 MW;  F288A117B8D45D55 CRC64;
     MSLKFILGTA SYDHHQALVT NLKATFQEKP QERYFYLVPN HIKFESEVSI LEALKSDEND
     YVAASQIQVF SLTRLAWYFM KNTPYYQIPR ISTAGLNMLV FRLLQEHQEQ LQLFRGEVRH
     TGFVAQLTKQ LLELKIGCIT PADLTAMAEN LGDQQVELAK KLHDLTIIAT AFEAAMQKRF
     IENTALIDAL TLFLQQQTLT DCHFYVEGFA QFTAQEQALL TTLMQQSEVQ IGFILDRAYP
     NQQPDGLNFF FQAGRTYYNL YQQARLNHVP VMMDQMADSQ RLTPALAALD QFWVSSESPG
     NRKLSPVPVA DHLHVVAAEN RYAELRYVAR EIRRLVQTGH YRYRDFLILT RHLAPYQTMI
     APILTEYEIP YFCDLPQTMA AHPLVSLLEK LLDVNLHFYR YEDVMALLKT ELLIPKGMSI
     AEFRADLDLC ENLILKNGYE GKDWLNDFDW QFYRFGSYQE GTRTTQDEAL TERINGIRRY
     VQATLPPFYR ALKAAKTGRQ VVQVLYQFLI DHGVDRQLLH WRDQALAANQ VAQAGQPEQT
     WSTFMQMLDE YVTLLGDVSF EEDNTEQLNE FKQLLSAGFA AAQYAQIPST LDQVVLSESG
     MVQTKKRQIT FMIGSTDQVM PDQIENTALL TDQDRQRLLD NEGQVTPLLN ESSVGKMNAE
     PYLNYLAFLS SQTTVYFTYP LGNGEGTAFK ISPYVERIRN HFDLTIQKIA AEQSLQSTET
     PQGSWRSLLS DLIQVSRQAQ ENQTLIPEQW LTTYRLLQQA PQSQFLTTQL FQSLNYRNEP
     ERLTPEIVTG LYGNEIHTSI SKLEEFYQNQ YAYFLKYGLK LQERPVFELT PANTGNFYHE
     VMDRFIKLIQ GQQIALPELD DQQIDKLVSE VLAKTYEQPE FKILNKTARM GYIRQQLMQT
     VKRVSLALRN QSLSTNLRPL ATEVLFGQVG AEKGLQGLNF MLDDHREVKV RGKIDRIDQL
     TINNQPYLGI VDYKSSQHSF NFRDAYYGLA LQMLTYLETV LQDQQAILPA NSAVKPAGAF
     YLHLKNPTLT LKQLTKKKMG QLQKGEFDQM LLDQFKYNGL IVNDEELLEN LDTTLVNGQS
     PLFAFSKLKS GKFSSKQLVT LNQLDLLMAH NEDLIKEAGQ AIFAGDTALN PIMRPDRTNA
     LTLSPFKSIF QFDAMLPENN YRQLEALDEK AVLERLMSKK GDGNLE