ID   ADDB_STRSV              Reviewed;        1093 AA.
AC   A3CNU0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=SSA_1452;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44845.1; -; Genomic_DNA.
DR   RefSeq; WP_011837145.1; NC_009009.1.
DR   RefSeq; YP_001035395.1; NC_009009.1.
DR   AlphaFoldDB; A3CNU0; -.
DR   SMR; A3CNU0; -.
DR   STRING; 388919.SSA_1452; -.
DR   PRIDE; A3CNU0; -.
DR   EnsemblBacteria; ABN44845; ABN44845; SSA_1452.
DR   KEGG; ssa:SSA_1452; -.
DR   PATRIC; fig|388919.9.peg.1377; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000002148; 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   HAMAP; MF_01453; AddB_type2; 1.
DR   InterPro; IPR014141; DNA_helicase_suRexB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02774; rexB_recomb; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1093
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379412"
SQ   SEQUENCE   1093 AA;  124150 MW;  373584913B38AAB5 CRC64;
     MKLLYTDIRH SLTKVLVAEA ESLVAAGKRV FYIAPNSLSF EKERSVLECL KTQASFAITV
     TRFAQMARYF VLNDVRQGQS LDDIGLGMLI YRTLTELDDG ELKVYSRIKK DPQFIQQLMD
     LYHELQTAQM SFADLEFLEE PEKREDLVKI FTAVTAALNK GDFDSSSQIA AFAQHILAGD
     TDEELADLAL VIDGFTRFSA EEEYLVGLLH RKGVEIVIGT YASQKAYRAA FREGNLYQAS
     VDFLRKLAED YQVKPDYIPH AEAEDAFGRI SKILESRYDF SESTVSLSES DRSQLQIWAT
     MNQKEELEYV AKSIRQRVHE GVRYKDIRLL LGDVEAYQLQ LKTIFDQYQI PYYLGRSESM
     AQHPLVQFVE SLERLKRYNF QLEDLLNLLK TGLYGDLTQE ELDHFEQYLR FADIKGAGKL
     AKDFTANSQG KFDLDCLNHI RRRVMTPLQD FFKSRSQTAS GLLAKFTEFV QAARLSDNLT
     ALLQGESQQE QERHEEVWKA FSHVLEQFAQ VFADSKVKLD DFLALVLSGM LLSNYRTVPA
     TVDVVKVQSY DLIEPLAAPY VYAIGLTQER FPKIAQNKSL LSDEDRARLN DATDSQAELQ
     IASSENLKKN RYTALSLMNS ATKELVLSAP ALVNEVEDSM STYLLELTAA PLSLPIIVKK
     PQASSDDIGS YRALLSQIIE LHQEEIDREW TAEEQTFWAV AVRVLRKKLA AEGISIPHIS
     KELKTETLQS ETLQALYPQE QPLRLSASAL NEYFRHQYAY FLKYVLRLQE EWTIHPDARS
     HGIFLHRIFE KVLQDDSSAD FDRRLAQAME ETSREAEFES IYSESGQTRF ARQLLLDTAR
     ATGRVLAHPS GIETIGEETG FGSASTPFLT LENGRAVTVS GKVDRIDRLT KTESLGVVDY
     KSGDIKFSFE KFFNGLNSQL PTYLAAIEEL ADYQEDKGTF GAMYLQMTDP IVALKDTKTL
     ADAVSQSMKP LQYKGLFVAD AVKELGPLYE KNKTNLLSQE DLDLLLAYNA YLYKKAAEGI
     LSGHFAVNPY TENGRSIAPY VEQFKAITGF EANLHLGQAR QLEKLDASKF DRRPTGDKLR
     QAWLEKMREE MEK