ID   ADDB_STRMU              Reviewed;        1080 AA.
AC   Q8DT75;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=SMU_1500;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59153.1; -; Genomic_DNA.
DR   RefSeq; NP_721847.1; NC_004350.2.
DR   RefSeq; WP_002262920.1; NC_004350.2.
DR   AlphaFoldDB; Q8DT75; -.
DR   SMR; Q8DT75; -.
DR   STRING; 210007.SMU_1500; -.
DR   PRIDE; Q8DT75; -.
DR   EnsemblBacteria; AAN59153; AAN59153; SMU_1500.
DR   KEGG; smu:SMU_1500; -.
DR   PATRIC; fig|210007.7.peg.1335; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; DRLENYV; -.
DR   PhylomeDB; Q8DT75; -.
DR   Proteomes; UP000002512; 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   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01453; AddB_type2; 1.
DR   InterPro; IPR014141; DNA_helicase_suRexB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
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..1080
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379393"
SQ   SEQUENCE   1080 AA;  123793 MW;  63A419D9A23B4751 CRC64;
     MKLLYTDIQY NMIDILAGEA QLAAKAGKRV FYIAPNSLSF EKERAVLETL PERASFAITI
     TRFEQMARYF VLNDIHQGET IDDNGLVMVF YRVLSSFSDQ DLRVFGRLKQ DAHFINQLVD
     LYKELKASNL TVLELNQLNS AEKQEDLIKI FTEVETILSA GHFDNQSKIA FFAQQIKFGH
     LDTALQDLTI VIDGFTRFSA EEENLIGLLH EKGVDIIIGT YISQKAYRST FSNGNVYQAS
     LDFIRGLAGK FQTKPEYVVS KQEALPAFTK LSQLFESCHD FSDSQLVLTD KDKEHVTIWD
     VINQKEEVEH VAKSIRRKLY EGHRYKDILV LLGDADAYKL QIGKIFDKYE IPYYFGKAES
     MSSHPLVHFV DSLERVKRYN FRAEDVMNLL KSGLYGKIRQ NQLDKLEQYV IYADIKGKTK
     FFKDFTLDNH GQFDLKALNK LRAEVMSPLQ ELIKIQAQKG DSILQKLTNF LEAISLTNNF
     SKLIQGVSDT EQEKNEQVWK TFTVILEQFH TIFGQEKMKL ADFLALLRSG MLAADYRTVP
     ASVDVVTVKS YDLVEPHSNK FVFALGMTQS HFPKIVQNKS LISDEERAKI NEATPDNRRF
     DIVTKENLKK NHFTALSLFN AATQELVLTL PQILNEAEDN TSSYLLELQD MGVPVVEKGG
     NRLAADPEDI GNYKALLSRV IELNRSAIDQ ELSKEEQTFW SVAVRYLRQK LAKEGLTIPE
     VNDKMQTKQV AAEVMAARFP IDQPLNLSSS ALTTFYNNQY LYFLQYILGL QELETIHPDA
     RNHGTYLHRV FELVMQDQST DDFDSKLNRA IDITNHEDSF HLVYNEDEES RYALGILEDI
     ARSTATVLKG DNPVQAESEE EAFELMLDQA VKIRGVIDRI DRLSDGSLGI VDYKSSKNTF
     DLQKFYNGLS PQLVTYIEAL RSCKNLNDTD KIFGAMYLHM QEPKTDLANM KSIEKIPETV
     HKNLSYKGLF LEDEKAHLAN GKYHLHDAVY SQKEVDLLLD YNKRLYRSAA KQIRKGNFLI
     NPYSQDGKSV QGEQLKAITH FEADRHMPYA RKLYQLPRKE KRQGFLALMQ SKKEEEGNDL