ID   ADDB_LACGA              Reviewed;        1158 AA.
AC   Q043G5;
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=LGAS_1032;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS   102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC   3163 / NCIMB 11718 / NCTC 13722 / AM63;
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; CP000413; ABJ60407.1; -; Genomic_DNA.
DR   RefSeq; WP_003647272.1; NZ_WBMG01000008.1.
DR   AlphaFoldDB; Q043G5; -.
DR   SMR; Q043G5; -.
DR   KEGG; lga:LGAS_1032; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   BioCyc; LGAS324831:G1G6Y-1032-MON; -.
DR   Proteomes; UP000000664; 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.
FT   CHAIN           1..1158
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379372"
SQ   SEQUENCE   1158 AA;  133949 MW;  A9C26B4CE688B3FE CRC64;
     MINVITGRQV DNLQNEIIDQ AVKSYYQDKT HDVFIIVPNH IKFTTEVRAL SKLSVLTNKK
     QVAVNKLHIL SFSRLAWYFL KDEAIKLPQI LDDAASVMLL EQIVKDHQDE LKLFQNKNQI
     TSGALRQMYE AILSVRAGNI DLENIDNEKL NEETSYKVHD LQIIYDDFID RLSEKFATKD
     EMQLLLNEFL AKSDSLSTMV FYFSDFSHFS LQELTSVRLI SKKAKNTTLA FKTKIGKIDS
     KAEQGDYDYV VQRTIRQLEH FWQNQQLNYQ TTEFPLTKTN PSSLLNGVWT KTNGFDESLS
     KFLQPVKADS RYAEAYFVAR TIYQQVALNN YRYQDFLVLA PNLNEYETYL TPILRQNNIP
     FFNDLQKEMK YHPLVVAVEN LQQIFKRGFQ TDNVIALMKT QLFIPEWYKS VARYQNDVDL
     LENFVLAHGI KGELWKKPLK SFVDAEVIAL DKSEQEVEEL DRLRKYFISI LSEFFEDIET
     EKDPQAGVTI FWNFLIKNRV AKRLEAWRKE ANDAGDLQLA QQPEQVWSTL NDLLKDYLLV
     AKEFSLEQFF DLLISGFSEA NFSQIPSTLD AVNISEMGMV QGQGYKQVFI IGATSSNLPQ
     IEKIPGFFSS ENLEQLNDGN NASGYLEDQQ KINNLDQNYQ FGNALSLASD KIYISYPVIN
     TANEQLEPSI FYKQLLRLTQ ANEFSQHDLP SSAGDLLTFM TNPEASLGYL TYLKGKQEVN
     VDSILELTEQ EIGEVAQNVL EGSNFKNVPE NLPPKLAQEL YGDRIETSVS QLETYYQNSF
     EYFLNYGLHL KKRFENELDV IQAGNYYHET FDYLVKKIKE KNLDFADLTD SKLNQLLIEV
     REELKEKGRY RQLLNDPFNK YLFHKLDQTT SNVAHYWHSN VNKTTFRPQY SELSFGKNQK
     VTGLSYSWKD ENNQKKIVDL RGKMDRVDLA KVNDRVLGEV IDYKSSAKKF DLGLFANGIS
     MQMISYLEVL KKNNKFFAQG KNLDVLGAFY QNITSSLERL SSDKMILSNY QIKDLLKEST
     KKLMYNGILV ADEEILDLIE PGMEKDRATS EIYSSIKRKV NGDISWPRNQ SFTPDQLELL
     LAYNSYLIKN AGSEILSGKI KLDPYTYGQQ SSLTYSDFKD IFFFDAMLKE NNYHKIKAID
     KKTLLNLIKE KLDLDGDE