ID   ADDB_STREM              Reviewed;        1073 AA.
AC   B4U2H0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 71.
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=Sez_0828;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACG62187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001129; ACG62187.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041785439.1; NC_011134.1.
DR   AlphaFoldDB; B4U2H0; -.
DR   SMR; B4U2H0; -.
DR   PRIDE; B4U2H0; -.
DR   EnsemblBacteria; ACG62187; ACG62187; Sez_0828.
DR   KEGG; sez:Sez_0828; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   Proteomes; UP000001873; 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_0000379391"
SQ   SEQUENCE   1073 AA;  122237 MW;  66B63219AF8FE89E 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 YSQLDWQLSA KDKSKVVIWQ
     ALNQKEELEH VTKAIREKLY QGYRYKDMLV LLGDVASYQL QIGPIFEKFE IPYYIGKQEP
     MSAHPLVQFV ESLERGRRYN WRREDIVNLL KSGLFGRFQE GELDQLEQYL VFADIQGFTK
     FSRPFTLNSS RQYPLPLLNQ LRLAVVTPLQ QLFKSQKQLG ASLLDKLMTF FKTIQLADNF
     EALAGSRREA DREKDEEVWK TFTGILETFY QVFGQEKMTL ADCLALIKMG MQTAHYRTVP
     ATLDVVSIKS YDLVEPHSKP FVFAIGLSRS HFPKQTKNTS LISDQERASI NEQTASYQRL
     DVPSFENIKK NHQTALSLFN AATQELVLSL PTSLTNSSDD VSPYLKELIA LGVPVIEKGK
     NRLSHSAADI GNYKALLSRL VAINRQGIAD DMTSEDRNFW TVALRYLKRR LADEQLSLPA
     FEHHLTTKPV APEVIETRFP SQQPLSLSSS ALTVFYNNQY KYFLKYVLGL QEPESIHPDA
     RIHGQYLHRI FELVTKDRSN 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 VLPAKERRQA FLTRMNEEIK HED