ID   ADDB_STRP8              Reviewed;        1071 AA.
AC   Q8P1J3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=spyM18_0835;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(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; AE009949; AAL97495.1; -; Genomic_DNA.
DR   RefSeq; WP_011017622.1; NC_003485.1.
DR   AlphaFoldDB; Q8P1J3; -.
DR   SMR; Q8P1J3; -.
DR   KEGG; spm:spyM18_0835; -.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; DRLENYV; -.
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.
FT   CHAIN           1..1071
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379404"
SQ   SEQUENCE   1071 AA;  124200 MW;  12AA359FD95D0A87 CRC64;
     MKLIYTEMSY SMTEILVNEA RKAADQGYRV FYIAPNSLSF EKEREVLTLL PERGTFSIIV
     TRFVQMSRYF TVESSPSKQH LDDTTLAMIF YRALMQLKPE DLPSYGRLQN NSVFIEQLVE
     LYKELKNAQL SVHDLTGLDH PQKQEDLIKI IELAETIMIQ QDYNQDSPLQ SFARAIKLGL
     LNNQLSKTVV VIDGFSRFSA EEDYLLSLLN NNCQEVIIGS YVSQKAYQKS FIKGNIYEAS
     LHFLQDLAQK YHIKPVFATS NQVFKPAFSR LTQLFEATHD FSQVDWQLQK NDLDHFSLWQ
     CHHQKEEIEH VAKSIRQKLY EGYRYKDILV LLGDMDAYQL QIGPIFDKFE IPYYLGKAEP
     MAAHPLVQFI ESLERSQRYN WRREDILNML KSGLFGCFDD SDIDRFEEYT QFADIKGFTK
     FSKPFTINSS RQYPLDFLNE MRQDIVLPLQ ELFKSQKQLG ASLVDKLILF LKKIRLAENM
     QGLAQSQLEV EKNEEVWKRF TDILTSFHHI FGQEKLRLSD CLALIKTGMK SAQYRVVPAT
     LDVVTIKSYD LVQPHSKPFV YAIGLTQSHF PKQIHHSGLL SDQERARINE IRNYRHFDIA
     SAENSKKNHQ TALSLFNAAT KELVLSVPTV INETFDDLSP YLKELINFGL PLLDKGKNYL
     SYDNSDIGNY KALLSQIIAI NRQDLIEMSD QDKMFWTVVL RYLRKQLRKQ QLELPTSDYR
     LSTKPLSKEV IEVCFPKGIP LKLSATALTV FYNNQYNYFL KYVLNLNKTE SIHPDSRIHG
     QYLHRVFERL MKDHTQEPFD NKLKQAIYHT NQESFFQQVY QDNAEAEYSL AILEDIVRST
     APILQLNQNI KVIDQEKNFH LDMGNEILVH GIIDRIDQLS DGSLGVVDYK SSANQFDIGT
     FYNGLSPQLV TYLAALKQIA PHDINQLFGA MYLHLQDPKL DLVTFKQIDN TLVESIYKAL
     TYKGIFSEVE KEHLSTGAYQ TKNALYSNDE LETLLNYNKY LYLKAVKHIK KGHFLINPYT
     SDGKTVQGDQ LKAITRFEAD LDMAQARRLV TLPAKEKKEC FLTLMRKESH L