ID   ADDB_STRA1              Reviewed;        1077 AA.
AC   Q3K1I5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=SAK_0996;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(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; CP000114; ABA44736.1; -; Genomic_DNA.
DR   RefSeq; WP_000772298.1; NC_007432.1.
DR   AlphaFoldDB; Q3K1I5; -.
DR   SMR; Q3K1I5; -.
DR   KEGG; sak:SAK_0996; -.
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; -; 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.
FT   CHAIN           1..1077
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379387"
SQ   SEQUENCE   1077 AA;  124020 MW;  B2C803A76476E038 CRC64;
     MKLLYTDINH DMTEILVNQA AHAAEAGWRI FYIAPNSLSF EKERAVLENL PQEASFAITI
     TRFAQLARYF TLNQPNQKES LNDIGLAMIF YRALASFEDG QLKVFGRLKQ DASFISQLVD
     LYKELQTANL SILELKYLHS PEKFEDLLAI FLVVSDLLRE GEYDNQSKIA FFTEQVRSGQ
     LDVDLKNTIL IVDGFTRFSA EEEALIKSLS SRCQEIIIGA YASQKAYKAN FTNGNIYSAG
     VDFLRYLATT FQTKPEFILS KWESKSGFEM ISKNIEGKHD FTNSSHILDD TAKDCITIWE
     CINQKDEVEH VARAIRQKLY QGYRYKDILV LLGDVDSYKL QLSKIFEQYD IPYYFGKAET
     MAAHPLVHFM DSLSRIKRYR FRAEDVLNLF KTGIYGEISQ DDLDYFEAYI SYADIKGPKK
     FFTDFVVGAK KFDLGRLNTI RQSLLTPLES FVKTKKQDGI KTLNQFMFFL TQVGLSDNLS
     RLVGQMSENE QEKHQEVWKT FTDILEQFQT IFGQEKLNLD EFLSLLNSGM MQAEYRMVPA
     TVDVVTVKSY DLVEPHSNQF VYALGMTQSH FPKIAQNKSL ISDIERQLIN DANDTDGHFD
     IMTQENLKKN HFAALSLFNA AKQELVLTIP QLLNESEDQM SPYLVELRDI GVPFNHKGRQ
     SLKEEADNIG NYKALLSRVV DLYRSAIDKE MTKEEQTFWS VAVRYLRRQL TSKGIEIPII
     TDSLDTVTVS SDVMTRRFPE DDPLKLSSSA LTTFYNNQYK YFLQYVLGLE EQDSIHPDMR
     HHGTYLHRVF EILMKNQGIE SFEEKLNSAI NKTNQEDVFK SLYSEDAESR YSLEILEDIA
     RATATILRQD SQMTVESEEE RFELMIDNTI KINGIIDRID RLSDGSLGVV DYKSSAQKFD
     IQKFYNGLSP QLVTYIDAIS RDKEVEQKPP IFGAMYLHMQ EPRQDLSKIK NLDDLVTKNH
     QALTYKGLFS EAEKEFLANG KYHLKDSLYS ETEIAILQAH NQSLYKKASE TIKSGKFLIN
     PYTEDAKTVD GDQFKSITGF EADRHMARAR ALYKLPAKEK RQGFLTLMQQ EEENDDL