ID   ADDB_STRPJ              Reviewed;        1091 AA.
AC   B8ZQ31;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=SPN23F10540;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/jb.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA   Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA   Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-resistant
RT   pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(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; FM211187; CAR68870.1; -; Genomic_DNA.
DR   RefSeq; WP_000772339.1; NC_011900.1.
DR   AlphaFoldDB; B8ZQ31; -.
DR   SMR; B8ZQ31; -.
DR   KEGG; sne:SPN23F10540; -.
DR   HOGENOM; CLU_007838_0_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   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.
FT   CHAIN           1..1091
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379395"
SQ   SEQUENCE   1091 AA;  124786 MW;  BCC794E9A194BD13 CRC64;
     MKLLYTDIRT SLTEILTREA EELVAAGKRV FYIAPNSLSF EKERAVLECL SQQASFSITV
     TRFAQMARYL VLNDLPAKTT LDDIGLGLAF YKCLAELDPK DLRVYGAIKQ DPQLIQQLIE
     LYHEMTKSQM SFLDLENLTD EDKRADLLLI FEKVTAYLNQ GQLAQGSQLS HLIEAIENDK
     VSSDFNQITL VIDGFTRFSA EEERVVDLLH GKGVEIVIGA YASKKAYTSP FSEGNLYQAS
     VKFLHHLASK YQTPAQDCSQ THEKMDSFDK ASRLLESSYD FSELALDVDE KDRENLQIWS
     CLTQKEELEL VARSIRQKLH ENSDLSYKHF RILLGDVASY QLSLKTIFDQ YQIPFYLGRS
     EAMAHHPLTQ FVESILALKR YRFRQEDLIN LLRTDLYTDL SQSDIDAFEQ YIRYLGINGL
     PAFQQIFTKS HHGKFNLERL NVLRLRILAP LETLFASRKQ KAENLLQKWS VFLKEGAVTK
     QLQDLTTTLE AVEQERQAEV WKAFCHVLEQ FATVFAGSQV SLEDFLALLH SGMSLSQYRT
     IPATVDTVLV QSYDLIAPLT ADFVYAIGLT QDNLPKISQN TSLLTDEERQ NLNQATEEGV
     QLLIASSENL KKNRYTMLSL VNSARKQLFL SAPSLFNESE SKESAYLQEL IHFGFRRREK
     RMNHKGLSKE DMGSYHSLLS SLVAYHQQGE MSDTEQDLTF VKVLSRVIGK KLDLQGLENP
     AIPTSPSSKT LAKDTLQALY PAKQEFYLST SGLTEFYRNE YSYFLRYVLG LQEELRLRPD
     ARSHGNFLHR IFERALQLPN EDSFDQRLEQ AIQETSQERE FEAIYQESLE AQFTKEVLLD
     VARTTGHILR HNPAIETIKE EANFGGKDQA FIQLDNGRSV FVRGKVDRID RLKANGAIGV
     VDYKSSLTQF QFPHFFNGLN SQLPTYLAAL KREGKQNFFG AMYLEMAEPV QSLMAVKSLA
     GAVVEASKSM KYQGLFLEKE SSYLGEFYNK NKANQLTDEE FQLLLDYNAY LYKKAAEKIL
     AGRFAINPYT ENGRSIAPYV QQHQAITGFE ANYHLGQARF LKKLDLADGK RLVGEKLKQA
     WFEKIREELN R