ADDB_LACAC
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 03-AUG-2022, entry version 80.
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=LBA1166;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; 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. {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; 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 PRIDE; Q5FJW9; -.
DR EnsemblBacteria; AAV43005; AAV43005; 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 OMA; DRLENYV; -.
DR BioCyc; LACI272621:G1G49-1156-MON; -.
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: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..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