ID   ADDB_LACAC              Reviewed;        1160 AA.
AC   Q5FJW9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 86.
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   AltName: Full=ATP-dependent helicase/nuclease subunit RexB {ECO:0000255|HAMAP-Rule:MF_01453};
GN   Name=rexB {ECO:0000255|HAMAP-Rule:MF_01453}; OrderedLocusNames=LBA1166;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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 but not helicase activity. {ECO:0000255|HAMAP-
CC       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   -!- MISCELLANEOUS: Despite having helicase-like domains, this subunit does
CC       not have helicase activity. {ECO:0000255|HAMAP-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; CP000033; AAV43005.1; -; Genomic_DNA.
DR   RefSeq; WP_011254367.1; NC_006814.3.
DR   RefSeq; YP_194036.1; NC_006814.3.
DR   AlphaFoldDB; Q5FJW9; -.
DR   SMR; Q5FJW9; -.
DR   STRING; 272621.LBA1166; -.
DR   GeneID; 56942767; -.
DR   KEGG; lac:LBA1166; -.
DR   PATRIC; fig|272621.13.peg.1108; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OrthoDB; 9758506at2; -.
DR   BioCyc; LACI272621:G1G49-1156-MONOMER; -.
DR   Proteomes; UP000006381; 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: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; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   HAMAP; MF_01453; AddB_type2; 1.
DR   InterPro; IPR049035; ADDB_N.
DR   InterPro; IPR014141; DNA_helicase_suRexB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   Pfam; PF21445; ADDB_N; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1160
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379365"
SQ   SEQUENCE   1160 AA;  134304 MW;  7D7C51AA3878B1C1 CRC64;
     MIKILTGRQT DPVQEKILEE AVKNYQQHPE NETFIIVPNH IKFTTEVRAI NKLATSKNKS
     ETAVKNLHVL SFSRLAWFFL KDAEQGLPTQ LDDAASAMLL THIIEKEKDN LTIFETINSG
     LVQQLYNTIL QMYDGNIDLD NIDETNLDQE TKSKIHDLRI IYDAYIKEIA GKFSTKNEVQ
     VELNKVLANN KSLSNASFYF CDFSHFSLQE TLTIKLLIRK AQNVILGFKT KLGDINPQAE
     AGDYDYVIQQ TIKRFTSFLQ ERNINYTVNN FPLSSKPTNR ENLNSLWTES INKVDNIKKH
     VQLVKADSRY AEAYFVARSI YQQVALGNYR YHDFLILAPD LKEYETYLTP ILRQNKIPFF
     NDLQQEMKYH PLVVLIESLF NMYDEKTISL NTQSIIAILK THLMIPSWYK EEAEFIHDVD
     ELENFVLAHG IEHNLWQRPF SHFVNAEVIR LDKMDEEIAK LNRLREFLIN KITELLEKLK
     KEESSQKALT MFFDFLTNNG IASRLEQWRN DANDAGDLQQ AQQPEQLWDL LIQLLKDYLM
     INPEKFDVDE FFNMLINAFR EANFSQIPST LDAVNLSELG MVQTGGYKQV FIIGATSGNL
     PAIQKTPGFL TPENINQLQN SFASDAYLED NQQLNNLDQN YQFGLALALA QDKVYVSYPI
     LNASNERLDS SIYYKRLFDY VDSEFEQHDL PEKFNDLLSF ITSADASLGY LSYINSIDSS
     KEFDELLRIT HEQSPQKTEI VLQASEFNNQ PEDIGQELAE KLYGQNLNSS VSQLETFYEN
     SYEYFLTYGL RLHRRLENEF DVIQAGNYFH ETFDRLVKQL NKEHIDLASL NSFELERMLN
     SVRNVMKNEG KYAQLMNDPF NEYLFKCLDH TTSKVAHNWC KNLNKTPLRA KYSELSFGVG
     EKLKGLSLDV PNLSGNHRVD LRGKMDRVDI AHLADKNQVL AQVIDYKSSA KKFDLSMFYN
     GIAMQMVSYL DILVKNNQFF AGNNELSLLG AFYQTVTRQL ERLNSNKLID SQLNIRDNVI
     DGKPKLMYTG LINNNPQVLT EAEPFLDNSS RQSELYSMVK TKKNGTFSLP TDRSFSEEEL
     ELLLEYDEFL IKEASNQILS GKIELNPYRQ GKSKSALTYS DYKDIFFFDA MLRQNQYHEI
     TRLSKKDLLS KIKERLGKED
//