ID   ADDB_LEUMM              Reviewed;        1159 AA.
AC   Q03W48;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-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=LEUM_1482;
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS   20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS   8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC   / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
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; CP000414; ABJ62574.1; -; Genomic_DNA.
DR   RefSeq; WP_011680161.1; NC_008531.1.
DR   AlphaFoldDB; Q03W48; -.
DR   SMR; Q03W48; -.
DR   STRING; 203120.LEUM_1482; -.
DR   EnsemblBacteria; ABJ62574; ABJ62574; LEUM_1482.
DR   KEGG; lme:LEUM_1482; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000362; 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; -; 4.
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..1159
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379384"
SQ   SEQUENCE   1159 AA;  130608 MW;  98F059E611151DC7 CRC64;
     MSLNVVMGNG QHDLRSEMLT MIQQQFCQNE LLTVFYIVPN HVKFDSEVNV LQRFSIMNGN
     DDSELYAQSR LQVYSLTRLA WALMKNTPDR QPDIVEPTGL FMIVSNILRE QSDNLPVFSR
     MQTKSGFVSA LVAQLVELRA SNVTPENLLE VLEKSADNIF LRQTLNAKLH DLAIVADDFN
     ARMGENQITG QETLIAFAKQ LADLKLSNVA FYFDGFNGFT SAEMMVVNQL ITTYPVTMGI
     LGDPEKMGQQ REGDVFFKPM TTVEQLSITA RTAQQEVAIT AATKMRPLSR TAQQVLGAWA
     CLGEYRNFTG SRDEVHLNVF AAENPITEIK EVARRIRRSL VDDPTLHLRD IIILSRDLTP
     YQAHIEAVMS QFELPYFLDM DVNMMNHPLV ELILNLLAPN KFQYQTMLAI LKTGLLRPTF
     ENKIVSHDEF FDIVSHMDNY LYAYRPYESR WRDFSRPFKL FQVTRDDDDT EISEDEKVNN
     RLEYLRHFIV EAFDELDDGF AMAKNLRQSV THLVLWLQKY HVTDALLEQR DDFIAQGNLS
     RSQQSEEVWQ MLTKTLDEMV EIDGERSVSL TDIVTTLQAG LSGAKFSGIP NNLDQLMISE
     AGIVQNTQYK QLYFIGGTRQ NLPAQVKNAA LINDAERSIV QPALQSGTNP RYLQNTAQQQ
     MAEENLLFYG SLMSSIGSIT LSYPILEPSG QLAEMSPFFK RLVDTFNSEV EVIGSIPSSA
     ASLLKQYVGT ARATLSDLVK ILPVYGQTAA FKAVQNVISN TMQDRLERVL SAPNYQNNTT
     KLKPEFISAL FGERLNVSIS QLESYYSNPF AYFLQYGLKL QERATNELNV AQTGTLYHAV
     FENVLHELIV KNKSLRDITG DELRALVRQH MQSQLALPAF EILNDSGKMR ATTNYLTRVC
     ETLVLNLQAA ARENTSKPEA VEQLFGFSKE SLPPLSFARM QVRGKLDRFD KQDVNGEFGT
     IIDYKSNGKT FNWGQAYDGL QMQLLTYWDA AQQSAEKLGV AAIGGAFFAK ISPEKTKITD
     KTDLNALFTG KLIPETFKYR GLFISEPAYV SALTTLEPQE KSAHYPVVLL KNGALGKIGV
     DAVDPDEFAL LLQRNRENII TAGDLILSGY FPIMPVEGGL TYSPYLDIIR FDRALGDAYK
     VQSPADKNTI IKLLKGGQD