ID   ADDB_STRPS              Reviewed;        1091 AA.
AC   B2IPX4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 77.
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=SPCG_1146;
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14;
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACB90398.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001033; ACB90398.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000772324.1; NC_010582.1.
DR   AlphaFoldDB; B2IPX4; -.
DR   SMR; B2IPX4; -.
DR   EnsemblBacteria; ACB90398; ACB90398; SPCG_1146.
DR   KEGG; spw:SPCG_1146; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   Proteomes; UP000001682; 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_0000379397"
SQ   SEQUENCE   1091 AA;  124746 MW;  8AB04FAF4C42A4C7 CRC64;
     MKLLYTDIRT SLTEILTREA EELVAAGKRV FYIAPNSLSF EKERAVLECL SQQASFSITV
     TRFAQMARYL VLNDLPAKTI LDDIGLGLAF YKCLAELNPK DLRVYGAIKQ DPQLIQQLIE
     LYHEMTKSQM NFLDLENLTD EDKRADLLLI FEKVTAYLNQ GQLAQGSQLS 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 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 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