ID   ADDB_STRP2              Reviewed;        1091 AA.
AC   Q04KF9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 89.
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=SPD_1015;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ55254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000410; ABJ55254.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000772372.1; NC_008533.2.
DR   AlphaFoldDB; Q04KF9; -.
DR   SMR; Q04KF9; -.
DR   STRING; 373153.SPD_1015; -.
DR   EnsemblBacteria; ABJ55254; ABJ55254; SPD_1015.
DR   GeneID; 60233988; -.
DR   KEGG; spd:SPD_1015; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OrthoDB; 1283891at2; -.
DR   BioCyc; SPNE373153:G1G6V-1103-MON; -.
DR   Proteomes; UP000001452; 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.
FT   CHAIN           1..1091
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379400"
SQ   SEQUENCE   1091 AA;  124854 MW;  02273B1E4ECF72A2 CRC64;
     MKLLYTDIRT SLTEILTREA EELVAAGKRV FYIAPNSLSF EKERAVLEYL SQQASFSITV
     TRFAQMARYL VLNDLPAKTT LDDIGLGLAF YKCLAELDPK DLRVYGAIKQ DPQLIQQLIE
     LYHEMTKSQM SFLDLENLTD EDKRADLLLI FEKVTAYLNQ GQLAQESQLS HLIEAIENDK
     VSSDFNQIAL VIDGFTRFSA EEERVVDLLH GKGVEIVIGA YASKKAYTSP FSEGNLYQAS
     VKFLHHLASK YQTPAQDCSQ THEKMDSFDK ASRLLESSYD FSELALDVDE KDRENLQIWS
     CLTQKEELEL VARSIRQKLH ENSDLSYKHF RILLGDVASY QLSLKTIFDQ YQIPFYLGRS
     EAMAHHPLTQ FVESILALKR YRFRQEDLIN LLRTDLYTDL SQSDIDAFEQ YIRYLGINGL
     PAFQQTFTKS HHGKFNLERL NVLRLRILAP LETLFASRKQ KAEKLLQKWS VFLKEGAVTK
     QLQDLTTTLE AVEQERQAEV WKAFCHVLEQ FATVFAGSQV SLEDFLALLH SGMSLSQYRT
     IPATVDTVLV QSYDLIAPLT ADFVYAIGLT QDNLPKISQN TSLLTDEERQ NLNQATEEGV
     QLLIASSENL KKNRYTMLSL VNSARKQLFL SAPSLFNESE SKESAYLQEL IHFGFRRREK
     RMNHKGLSKE DMGSYHSLLS SLVAYHQQGE MSDTEQDLTF VKVLSRVIGK KLDQQGLENP
     AIPTSPSSKT LAKDTLQALY PAKQEFYLST SGLTEFYRNE YSYFLRYVLG LQEELRLHPD
     ARSHGNFLHR IFERALQLPN EDSFDQRLEQ AIQETSQERE FEAIYQESLE AQFTKEVLLD
     VARTTGHILR HNPAIETIKE EANFGGKDQA FIQLDNGRSV FVRGKVDRID RLKANGAIGV
     VDYKSSLTQF QFPHFFNGLN SQLPTYLAAL KREGEQNFFG AMYLEMAEPV QSLMAVKSLA
     GAVVEASKSM KYQGLFLEKE SSYLGEFYNK NKANQLTDEE FQLLLDYNAY LYKKAAEKIL
     AGRFAINPYT ENGRSIAPYV QQHQAITGFE ANYHLGQARF LEKLDLADGK RLVGEKLKQA
     WLEKIREELN R