ID   ADDB_STRGC              Reviewed;        1093 AA.
AC   A8AY34;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=SGO_1414;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(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; CP000725; ABV09897.1; -; Genomic_DNA.
DR   RefSeq; WP_012130499.1; NC_009785.1.
DR   AlphaFoldDB; A8AY34; -.
DR   SMR; A8AY34; -.
DR   STRING; 467705.SGO_1414; -.
DR   EnsemblBacteria; ABV09897; ABV09897; SGO_1414.
DR   KEGG; sgo:SGO_1414; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000001131; 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_0000379392"
SQ   SEQUENCE   1093 AA;  124541 MW;  D0CAD840BE8D8439 CRC64;
     MKLLYTDIRH SLTKVLVAEA ESLVATGKRV FYIAPNSLSF EKERAVLECL KTKASFAITV
     TRFAQMARYF VLNDVRKGQS LDDIGLGMLI YRTLTELDDG ELKVYGRIKK DPQFIQQLMD
     LYHELQTAQM SFADLEFLEE PEKREDLVKI FTAVATALNK GDFDSSSQIA TFAQHILSGD
     TDEELADLAL VIDGFTRFSA EEEYLVGLLH RKGVEIVIGT YASQKAYRAA FRDGNLYQAS
     VDFLRKLAED YQVKPDYIPY AEAEDAFGRI SKVLESRYDF SEPAVEVSET DRSQLQIWAT
     MNQKEELEYV AKSIRQRVHD GVRYKDIRLL FGDVEAYQLQ LKTIFDQYQI PYYLGRSESM
     AQHPLVQFVE SLERLKRYNF QLEDLLNLLK TGIYGDLTQE ELDHFEQYLR FADIKGAVKL
     AKDFTANSQG KFDLDRLNHI RRRVMAPLQD FFKSRSQTAS GLLAKFTEFV QAARLSDNLT
     ALLQEESHQE QERHEEVWKA FSHVLEQFAQ VFADSKVKLD DFLALVLSGM LLSNYRTVPA
     TVDVVKVQSY DLIEPLAAPY VYAIGLTQER FPKIAQNKSL LSDEDRARLN DATDSQAELQ
     IASSENLKKN RYTALSLMNS ATKELVLSAP ALVNEVEDSM STYLLELTAA PLSLPIIVKK
     PQASSDDIGS YRALLSQIIE LHQEEIDREW TAEEQTFWAV AVRVLRKKLA AEGISIPQIS
     KELKTESLQP ETLHALYPKD QPLRLSASAL SEYFKNQYGY FIKYILGLQE EWTIHPDARS
     HGNFLHRIFE KVLQEDTSRD FDQRLEVAID ETMRETEFES LYNESSESLF TRQLLLDTAK
     STGQVLAQSA GIETIGEETV FGNSKEPFLI LEDGRAVSVR GKVDRIDRLL ADGSLGVVDY
     KSSETKFSYE KFFNGLNSQL PTYLAAIQEL QGQQEGRDLF GAMYLQMTEP IVALKDTKEL
     GDAVKEVAKT MQYKGLFLAD KLASLGPVYE KSKVNSLSQE ELAVLLAYNE ILYKKVAEGI
     LAGHFEVNPY TENGRNIAPY VDQFKAITGF EANRHLGQAR QLDKLDLSKF EKRPVGEKLR
     RAWIEKMREE LEK