ID   ADDB_STRSY              Reviewed;        1088 AA.
AC   A4VUD1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=SSU05_0754;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(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; CP000407; ABP89720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VUD1; -.
DR   SMR; A4VUD1; -.
DR   STRING; 391295.SSU05_0754; -.
DR   EnsemblBacteria; ABP89720; ABP89720; SSU05_0754.
DR   KEGG; ssu:SSU05_0754; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000000243; 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..1088
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379413"
SQ   SEQUENCE   1088 AA;  124466 MW;  6C2B5A3E6A05486F CRC64;
     MKLVYTDIRN PLTQYLTEQT ATFAEQGKRV FYIAPNSLSF EMERKVLEYL PEQATFDIIV
     TRFGQLARYL MIDRKEAGQP LDDVGLAMIF FRVLSQFEDG DLKVYGRLQT DFGFINQLVA
     LYKELQRANM SILDLEAMDS PDKQADLVKI FLAVTDILSK EGFEHQSKLA QLTGLVETGQ
     LDEQLKNIVL VVDGFSRFSA EEEALVSALN ERVSEILIGV YASKKAVQAT YAEGNVYQAN
     VDFLRQLSAQ FQTKATYIGQ EPVLDSIGKF SKNMEAYYDY SGTMIDLTPA DQEKIQLWEV
     VNQKEEVEQV ATAIRQHVHQ GARYKDILLL LGDVDSYKLQ IGKIFDKYDI PYYFGKAEEM
     SHHPLVHFVE SLERLRRYRF RAEDLLNLLK SGLYASISQK ELDLFESYIL FADMKGQAAF
     SRAFSVNGRA DYDAEVIKEK RLVYDLTVLE PLRAKIMEPL NQLFKAGPQS GTALLEKFMA
     FLEAIDLPKN MEKMSRNLSE VEQEKEEQVW KSFTHLLENF HQIFGKEKLK MDDFLAILQA
     GMQASHYRTV PATVDVVNVK SYDLIEPHTA KYVYAIGMGQ SNFPKVAKNT SLLTEEEMEK
     VNLVSASSSR FDLVSRENIK KNHAAMMSLL NSATEQLVIS TPQIYNEGED SLSPYIKILQ
     KMGLKSEERG RIKTLSPQDI GHYKSLLSRL IESERPSLET EEWEGQRAFW TVLVRHLKKK
     LESQSIEIPT ITGDIASKQL SDETLAALYP EDKPLNLSAS SLTNFYNNQY LYFVRNVLRL
     REQESIHPTA FQHGLFLHRI FERVVMDQSE LDFDQKVDKA ILRTRDEAEF AMFYNQDADA
     RYTEEVLDKI ARSSATILRD NDLVEIDGQE KSFRQDKALV FDLQNGKSVH VNGTIDRLDT
     LQINQAVGVV DYKSSDQSFS VGDFYNGLKP QLVTYLAALQ ELDETKDKPV FGAMYLHLQD
     PIIKLKDTKN LEQLEGAANT SLVYKGLFLK EESLGLNHFY QTRNQLYTED EFAVLLNHNQ
     ELYKQAAMDI LAGRFAINPY TKDGRSVAGE QLKAITGFEA DRHMGMARRL VKEAKRQDWM
     ERMKGGQD