ID   ADDB_STRS7              Reviewed;        1073 AA.
AC   C0MGY7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=SZO_11330;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204884; CAW99552.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MGY7; -.
DR   SMR; C0MGY7; -.
DR   EnsemblBacteria; CAW99552; CAW99552; SZO_11330.
DR   KEGG; seq:SZO_11330; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_1_0_9; -.
DR   OMA; DRLENYV; -.
DR   Proteomes; UP000001368; 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   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..1073
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379390"
SQ   SEQUENCE   1073 AA;  122255 MW;  73132DB8E7AEAB04 CRC64;
     MKLLYTEISY SMTEILVKEA RAYADKGYRV FYIAPNSLSF EKERSVLALL PEQGSFAITV
     TRFEQMARYF TLAKAANRQA LDDNGLAMIF YRVLMQLQED ELKVFHRLRT DQAFIAQLVE
     LYKELQAANL TAFDLTTLDR PEKQEDLITI MTKAEQLIAQ GDYDQSSRLA QLAEAIKSKS
     LDDELRQTVL VIDGFTRFSA EEEQLLALLN EACEEIVIGA YISQKAYRLA FTKGNLYEAS
     LAFIQQLAQQ FQTKPIYTTS EKVFDVSFSR LTQLLEANHD YSKLDWQLSA KDKSKVVIWQ
     ALNQKEELEY VAKAIREKLY QGYRYKDMLV LLGDVASYQL QIGPIFEKFE IPYYIGKQEP
     MSAHPLVQFV ESLERGRRYN WRREDIVNLL KSGLFGRFQE GELDQLEQYL VFADIQGFTK
     FSRPFTLNSS RQYPLPLLNQ LRLAVVTPLQ QLFKSQKQLG ASLLDKLMTF FKTIQLADNF
     EALAGSRREA DREKDEEVWK AFTGILETFY QVFGQEKMTL ADCLALIKMG MQTAHYRTVP
     ATLDVVSIKS YDLVEPHSKP FVFAIGLSRS HFPKQTKNTS LISDQERASI NEQTASYQRL
     DVPSFENIKK NHQTALSLFN AATQELVLSL PTSLTNSSDD VSPYLKELIA LGVPVIEKGK
     NRLSHSAADI GNYKALLSRL VAINRQGIAD DMTSEDRNFW TVALRYLKRR LADEQLSLPA
     FEHHLTTKPV APEVIETRFP SHQPLSLSSS ALTVFYNNQY KYFLKYVLGL QEPESIHPDA
     RIHGQYLHRI FELVTKDRTD AAFDQKLGAA IAAVNQQSAF QQVYQADAEG RYSLEVLKGI
     AYSTAPVLNL NQGMQVAKQE EAFELALGHQ ALIRGVIDRI DQLADGRLGI VDYKSSARVF
     DIGAFYNGLS PQLVTYLAAL KNKGQGLFGA MYLHMQEPRL SLSDFKVLDD QLVAAAYKEL
     TYKGIFLAQA KEYLANGSYH LNNTLYETDE LETLLAYNEQ LYLSAVKQIK TGHFLINPYT
     ADGKSVQGDQ LKAITRFEAD LDLGYARRLV VLPVKERRQA FLTRMNEEIK HED