ID   ADDB_LACJO              Reviewed;        1158 AA.
AC   Q74JA5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=LJ_1204;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09025.1; -; Genomic_DNA.
DR   RefSeq; WP_011162033.1; NC_005362.1.
DR   AlphaFoldDB; Q74JA5; -.
DR   SMR; Q74JA5; -.
DR   STRING; 257314.LJ_1204; -.
DR   PRIDE; Q74JA5; -.
DR   EnsemblBacteria; AAS09025; AAS09025; LJ_1204.
DR   KEGG; ljo:LJ_1204; -.
DR   PATRIC; fig|257314.6.peg.1070; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000000581; 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; Reference proteome.
FT   CHAIN           1..1158
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379374"
SQ   SEQUENCE   1158 AA;  134145 MW;  6B9EF9575C6D1D09 CRC64;
     MINVITGRQV DNLQNEIIDQ AVKSYYQDKR HDVFIIVPNH IKFTTEVRAL SKLSVLTNKK
     QVAVNKLHIL SFSRLAWYFL RDEAIKLPQI LDDAASVMLL EQIVKDHQDE LKLFQNQTQV
     TSGALRQMYE AILSVRAGNI ELDNIDEKKL NEETSYKIHD LRIIYDEFIE RLSEKFATKD
     EMQLLLNQFL AKSNNLSTME FYFSDFSHFS LQELTSVRLI SKKAKNTTLA FKTKIGKIDN
     NAEPGDYDYV VQRTIGQLEH FWQNQQLDYQ TQEYPLTQTS PSSLLNGVWT KTSGFDERLS
     KFLQPVKADS RYAEAYFVAR TIYQQVALNN YRYQDFLVLA PNLSEYETYL TPILRQNQIP
     FFNDLQREMK YHPLVVAVEN LQQIFKRGFQ TDNVIALMKT QLFIPDWYKN SARYQNDVDL
     LENFVLAHGI KGKLWTKSLK SFVDADVIAL DKSEKEVEDL DRLRDYFIDA LTKFFEQLDK
     EEDPQAGVTV FWNFLIKNRV AKRLESWRKE ANDTGDLQLA QQPEQVWSTL TDLLKDYLLV
     ANKFSVDQFF DLLISGFSEA NFSQIPSTLD AVNISELGMV QGQGYKQVFI IGATSTNLPQ
     IEKIPGFFSS ENLEQLNEGN EANGYLEDQQ KINNLDQNYQ FGNALSLASD KIYISYPVIN
     TANEQLEPSI FYKQLLKLTR ADEFAQHDLP QNNGEVLTFI TNPEASLGYL TYLKNKAATD
     VDSLLKMTEE KIGEVAKNVL EGSSFKNIPQ DLSPELAQQL YGDRIETSVS QLETYYQNSF
     EYFLNYGLHL KKRFENELDV IQAGNYYHET FDYLVKRIKE KKLNFADLTE EKLGELLIEV
     REELKEKGRY RQLLNDPFNK YLFHKLDQTT ANVAHYWHSN VNKTTFRPQY SELSFGKNQK
     VSGLSYSWKD DNNKKKIVDL RGKMDRVDLA QVNDRVLGEV IDYKSSAKKF DLGLFANGIS
     MQMISYLEVL KNNNKFFAQG KDLDVLGAFY QNITSSLERL SSEKMILSNY QIKDLAKEST
     KKLMYNGILI ADEEMLDLIE PGMEKDRAVS DLYTSVKRKV NGYISWPQNQ SFTPDQLDLL
     LAYNSYLIKN AGNEILSGKI ELDPYSYGQQ TSLTYSDFKD IFFFDAMLKE NNYHKIKSID
     KKTLLTLIRE KLDLDGEE