ADDB_STRPI
ID ADDB_STRPI Reviewed; 1091 AA.
AC B1IBR5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=SPH_1225;
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000936; ACA36414.1; -; Genomic_DNA.
DR RefSeq; WP_000772379.1; NC_010380.1.
DR AlphaFoldDB; B1IBR5; -.
DR SMR; B1IBR5; -.
DR EnsemblBacteria; ACA36414; ACA36414; SPH_1225.
DR GeneID; 66806234; -.
DR KEGG; spv:SPH_1225; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000002163; 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_0000379398"
SQ SEQUENCE 1091 AA; 124819 MW; DBF89A700311B558 CRC64;
MKLLYTDIRT SLTEILTREA EELVAAGKRV FYIAPNSLSF EKERAVLEYL SQQASFSITV
TRFAQMARYL VLNDLPAKTT LDDIGLGLAF YKCLAELDPK DLRVYGAIKQ DPQLIQQLIE
LYHEMTKSQM SFLDLENLTD 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 AVEQERQTEV WKAFCHVLEQ FATVFAGSQV SLEDFLALLH SGMSLSQYRT
IPATVDTVLV QSYDLIAPLT ADFVYAIGLT QDNLPKISQN TSLLTDEERQ NLNQTTEEGV
QLLIASSENL KKNRYTMLSL VNSARKQLFL SAPSLFNESE SKESAYLQEL IHFGFRRREK
RMNHKGLSKE DMGSYHSLLS SLVAYHQQGE MSDTEQDLTF VKVLSRVIGK KLDLQGLENP
AIPTSPSSKT LTKDTLQALY PAKQEFYLST SGLTEFYLNE YSYFLRYVLG LQEELRLRPD
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