ADDB_STRPN
ID ADDB_STRPN Reviewed; 1091 AA.
AC Q97QQ0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SP_1151;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=R6 / R800;
RX PubMed=15256582; DOI=10.1099/mic.0.27106-0;
RA Halpern D., Gruss A., Claverys J.-P., El-Karoui M.;
RT "rexAB mutants in Streptococcus pneumoniae.";
RL Microbiology 150:2409-2414(2004).
CC -!- FUNCTION: Involved in DNA double-strand break repair. Is not involved
CC in recombination during natural competence or in plasmid establishment.
CC {ECO:0000269|PubMed:15256582}.
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:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow poorly, are more
CC sensitive to UV light than wild-type cells and have reduced double-
CC strand exonuclease activity. {ECO:0000269|PubMed:15256582}.
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; AE005672; AAK75260.1; -; Genomic_DNA.
DR PIR; C95133; C95133.
DR PIR; G98001; G98001.
DR RefSeq; WP_000772372.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97QQ0; -.
DR SMR; Q97QQ0; -.
DR STRING; 170187.SP_1151; -.
DR EnsemblBacteria; AAK75260; AAK75260; SP_1151.
DR GeneID; 60233988; -.
DR KEGG; spn:SP_1151; -.
DR eggNOG; COG3857; Bacteria.
DR OMA; DRLENYV; -.
DR PhylomeDB; Q97QQ0; -.
DR BioCyc; SPNE170187:G1FZB-1170-MON; -.
DR Proteomes; UP000000585; 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_0000379394"
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
