ID   ADDB_LACDB              Reviewed;        1179 AA.
AC   Q04AN8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=LBUL_0907;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000412; ABJ58484.1; -; Genomic_DNA.
DR   RefSeq; WP_011678226.1; NC_008529.1.
DR   AlphaFoldDB; Q04AN8; -.
DR   SMR; Q04AN8; -.
DR   KEGG; lbu:LBUL_0907; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   BioCyc; LDEL321956:LBUL_RS04330-MON; -.
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; -; 4.
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   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 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_0000379370"
SQ   SEQUENCE   1179 AA;  134665 MW;  B1C4E58CAA1AEAC2 CRC64;
     MIKIITGRQS DPLQTEIIGR AARNYLAQPG KDTFIIVPNH IKFNTEVSAI GKVAQLQGRE
     ETSVKNLHVL SFSRLAWFFF KKADLLMPES LDDAAATMIL EQIIDKRRDE LLLFKNSHAN
     SGMIKQVYST ILQVHTGQLD LGNLLERAAD PAVALDLDNE TRDKLHDLDL IYQDFLEIVS
     EKHFATKDEL NIQLNQLLAS RPDLVSQASF YVTDFSHFSI QEKMTMQLLA AFASEMTFAF
     KTADGSVIEP AAGEYDYVVQ KTIKDLTGYF SAHDFAWERE KIASPASPAR DLNQAWQGQG
     QPDLNNLQLV KADSRYAEAY FVARTIYDEV ALKGCQYRDF LVLAPNLQEY ETYLAPILRQ
     NQIPFFDDLQ QQMKYHPLVL LLENLGKLLQ QAGDTPALLS IMKTRLLIPD WYLEGDAEAG
     EAAYLRDIDQ LENFALAHGI KYSLWQKPLK DFTKAQVIAL DQEQYQKWLD RLDKLRDFFV
     SKISRLARQL KSEKDSMTAV KLFFDFLVKN GVSARLEAWR LKASESGDLQ QAQQPEQCWN
     LLLSLLKDYL LVNPENFAWA DFFKMLTAAF SQANFATIPA SLDAVTLSEY GMVQTSGYKQ
     VFIIGAANGS LPQINDQPNF LTTENLASLA DFFDQDAYLE DSQQLRNLDQ EYQFGNALAL
     ASDRVYISYP VINSNNDLLD PSIYYKRLLK LVNGREYRQR DLPDIAEKDR TEFARQLLLF
     LTSPRASLGY LAYAEENSAQ SPLVAKLVEL SRQYEEEKAE EIAEGMAYDN NPQDISEDLA
     ERLYGKDLLS SVSQLESYYQ NSFEYFLNYG LRLRPRAENE LNAIQSGNYF HRTFELLLKE
     MQKKNIEIDK LSELDLELLL KQVRSEILQE PLYQQFLRDP FNEYLFKVFD KTTSKVAQSY
     RRKQQENKMR ATYGELAFGP AEKLAGLVLP LKKFAGQRKI SLRGKIDRVD LFNGDQHVLG
     QLIDYKSSDH SFNLARFASG VDLQMIAYLD VLEKNRDLLA GGRQFDLLGA FYQYVTRKLN
     SVNSSSTGAL FDSKLQLKEN LLGGEDKLKL SGVFVSEPAW YQEVDKALEK KATSSVYRGL
     KLNKSGGFGK KDNFFSQDEM RELLEYVEAL IEDAASEILS GQIALNPFRQ GNNTGLAFSD
     YKDIFYFDQQ LPTNSYRDLP NLKKADLLAL VEKRLRQRE