ID   ADDB_LACCB              Reviewed;        1179 AA.
AC   B3WEJ2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=LCABL_17120;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66793.1; -; Genomic_DNA.
DR   RefSeq; WP_012491617.1; NC_010999.1.
DR   AlphaFoldDB; B3WEJ2; -.
DR   SMR; B3WEJ2; -.
DR   KEGG; lcb:LCABL_17120; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
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.
FT   CHAIN           1..1179
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379368"
SQ   SEQUENCE   1179 AA;  131712 MW;  B3AC181C32F5DB14 CRC64;
     MGLQFILGDA TTDHAGTMAT MVQANLQADS QNQIFYLVPN HIKFEAEVDL LKRLRAQAAS
     VNGVYAQNRV QVLSFSRLAW YFLKNTALYQ QPRLDRASNT MLVAKILGES KEELTIYAGE
     AHNTGFVTQL ADQLSELVTG RITAEDLNTT VAALTPGDRH RAKLRDLGII LDHYEAEIGP
     YATNASLLSG LQQVMRNQDL SHTFIYLNDF NVFSASETGL VETMIETAAE VTVSLVLNKP
     YPAAPPVAPN LFLPAGRLYH RLYQKAKTMK VPIRLDRFAK PRPLSEGMNH LADWWQTSTN
     LQPQAPAQTA QNKEVELAVA TDPYHELRTV ARQIYQAVRQ GARYRDFLIL ARRLDPYAAV
     IPAIFEEFNI PQFTDLERPM KDHPLVVLIE SLFAIQDHDY QYQDVMRLLH TELLLPENMD
     IAAFRDALDT TDNHLVRTGI TGKKRWTQTD PWRYFQRNPN ADDSQLDPEA DKTAQINAIK
     TLVADTVPQL LRQWQTAKTG REAAASLYQW LQTTGVIDQL NVWRQTANAD GDLSRSQANE
     QAWDTFTQLL NDYATILGEA DFNRDQFREL LAAGFASATY TQIPSTLDSV VISETGLVRL
     AKAKHVYVIG ATNTAMPDVP NDSGVLNSEE RQLLAAQLPD DRFLPEQGPT TTLGDPFINY
     LGFMAASEKL TLSYPMQNTQ ENSENQASPY FRQLAQALQL TPATWAPAGL GTSLKAVLGS
     PRAMLSDFVR AAGEAQHQKL PLSRSWQGVL ASLKQTKLAP LAQKLAGSLT YQNNPGRLDP
     TLAVQLYGRD MNVSVSRLET YYRNQFEYFL KYGLLLQPRP EFELSPADTG SLFHAVLDQY
     LTQLRDAGQT LADVTAADVA AAVPPLVAAI TKRPGYEILG STHRMAYLTS RLSRLLIQVL
     TNMRQQQRRT GFRPMRTELQ FGQIGDTRGL PGLSWPLPHG GRVNVRGKID RLDVYRESDA
     QRFMVVDYKS TQHRFDDSDA YYGIALQMLT YVEAMANVPA DPPFVPAGAL YFHLQDPKFK
     FSTDLDLDID RLKAFKYLGF LVAKDGADLA AVDKTISAET GGRSMMVPLG FKKDGAFNYN
     QSNILTPEDL SAYLLHNQAL IIDAASRILA GDIALAPFQY GQESTVISNS DYQSIMLFDP
     ATGFDHYNHV PKLKRKEVLG RVTTDPTQIP HHRQEDSQA