ID   ADDB_STRT2              Reviewed;        1106 AA.
AC   Q5M2T6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=stu1717;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(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; CP000023; AAV61316.1; -; Genomic_DNA.
DR   RefSeq; WP_011226521.1; NC_006448.1.
DR   AlphaFoldDB; Q5M2T6; -.
DR   SMR; Q5M2T6; -.
DR   STRING; 264199.stu1717; -.
DR   EnsemblBacteria; AAV61316; AAV61316; stu1717.
DR   GeneID; 66899454; -.
DR   KEGG; stl:stu1717; -.
DR   PATRIC; fig|264199.4.peg.1689; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000001170; 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   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..1106
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379415"
SQ   SEQUENCE   1106 AA;  126737 MW;  AE537223FF818065 CRC64;
     MKLLYTDMSQ DLTEILTEQA SSYAQKGKRV FYIAPSALSF EKERKVLEYL PQSASFDITV
     TRFTQMARYF ILNTSNPKTQ LDDTGLAMIF YKVLLHMGDD ELKVYGRLRK DSNFINQLVD
     LYKELQQANM TVLDLQHLDQ VEKQEDLVRI FSAAQDLLLA GDFDNQSKLS AFFKEITSGH
     LDEALSNTVL VIDGFTRFSA EEEALVALLN DKCHQIVVGT YTSQKAYKAN FVYGNVYQAS
     VDFLRTLAQT YKVIPDYVTT DKEGNLSFAR ISRLLESRHD FSTVDETVTE QDKHALKVWE
     VVNQKEEVAQ VAKSIRQLLA DGKRYKDILV LLGDEESYKL HVGQIFRKFD IPYYFGKEES
     MSSHPLVEFV DSLERIKRYN YRAEDLLNLV KSGLYGGFAQ EDLDLFEYYV NFADIKGRHK
     FLSDFTANSR DKYNLDQINA LRSQLIEPLD KFLNSRKQKG SSLLKKLVVF LEAVQLPSQM
     FELSTKASEA EKEQNEQVWK AFTHILEQVE TIFGDESLSV DDFLSILRSG MLACDYRTVP
     ATVDVVNVKK YDLIQPHSAP YVFALGMTQS HFPKVGQNKS LLSDEERSRI NEATDEHRRL
     DIVTQINSKR GHFVAMSLFN AASEQLVLSQ PQIINESQDD MSVYLKELLD LGIPLVEKGR
     NRFEAKGDQI GNYRDLLSTV IALNSSHLDL DLDKETQTFW SVAVRYLRKR LDKDQVLIPK
     VIDDVTTTKV DDQVMQLVFP EEEPLKLSAT ALTTFYNNQY LYFLRYVLEL EELESIHPDA
     RHHGTYLHRV FERVMGDSSS ESFDDKLEKA IAQTNQDQPF EILYTEDQES RFSRQILEDI
     ARSTASVLRD NAAVKVECEE VKFDLLLANS IKITGIIDRV DRLTDGALGV VDYKTGKNVF
     DIQKFYNGLS PQLVTYLEAL RQTYKVDADQ LFGAMYLHMQ VPQLNLSQIG LEKLAAQAHK
     ELTYKGLFVA SETEHLTGGN YDLQKTVTYD KEDLETLLDY NIKLFRSAAE VIRSGNFAIN
     PYTEDGKSVQ GDQIKSITHF EADRHMGQAR KLLRLPKKGK KEAYLELMAK TEEENQMQVS
     ENTISFPVID HAVRVDKKDQ EDNHVD