ADDB_STRT1
ID ADDB_STRT1 Reviewed; 1106 AA.
AC Q5LY79;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-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=str1717;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV63237.1; -; Genomic_DNA.
DR RefSeq; WP_011227532.1; NC_006449.1.
DR AlphaFoldDB; Q5LY79; -.
DR SMR; Q5LY79; -.
DR PRIDE; Q5LY79; -.
DR KEGG; stc:str1717; -.
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; -; 3.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01453; AddB_type2; 1.
DR InterPro; IPR014141; DNA_helicase_suRexB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
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..1106
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379417"
SQ SEQUENCE 1106 AA; 126709 MW; E7B9562C3E603747 CRC64;
MKLLYTDMSQ DLTEILTEQA SSYAQKGKRV FYIAPSALSF EKERKVLEYL PQSASFDITV
TRFTQMARYF ILNTSNPKTQ LDDTGLAMIF YKVLLHMGDD ELKVYGRLRK DSNFINQLVD
LYKELQQANM TVLDLQHLDQ VEKQEDLVRI FSAAQDLLLA GDFDNQSKLS AFFKEITSGH
LDEALSNTVL VIDGFTRFSA EEEALVALLN DKCHQIVVGT YTSQKAYKAN FVYGNAYQAS
VDFLRTLAQT YKVIPDYVTT DKEGNLSFAR ISRLLESRHD FSTVDETVTE QDKHALKVWE
VVNQKEEVAQ VAKSIRQLLA DGKRYKDILV LLGDEESYKL HVGQIFRKFD IPYYFGKEES
MSSHPLVEFV DSLERIKRYN YRAEDLLNLV KSGLYGGFAQ EDLDLFEYYV NFADIKGRHK
FLSDFTANSR DKYNLDQINA LRSQLIEPLD KFLNSRKQKG SSLLKKLVVF LEAVQLPSQM
FELSTKASEA EKEQNEQVWK AFTHILEQVE TIFGDESLSV DDFLSILRSG MLACDYRTVP
ATVDVVNVKK YDLIQPHSAP YVFALGMTQS HFPKVGQNKS LLSDEERSRI NEATDEHRRL
DIVTQINSKR GHFVAMSLFN AASEQLVLSQ PQIINESQDD MSVYLKELLD LGIPLVEKGR
NRFEAKGDQI GNYRDLLSTV IALNSSHLDL DLDKETQTFW SVAVRYLRKR LDKDQVLIPK
VIDDVTTTKV DDQVMQLVFP EEEPLKLSAT ALTTFYNNQY LYFLRYVLEL EELESIHPDA
RHHGTYLHRV FERVMGDSSS ESFDDKLEKA IAQTNQDQPF EILYTEDQES RFSRQILEDI
ARSTASVLRD NAAVKVECEE VKFDLLLANS IKITGIIDRV DRLTDGALGV VDYKTGKNVF
DIQKFYNGLS PQLVTYLEAL RQTYKVDADQ LFGAMYLHMQ VPQLNLSQIG LEKLAAQAHK
ELTYKGLFVA SETEHLTGGN YDLQKTVTYD KEDLETLLDY NIKLFRSAAE VIRSGNFAIN
PYTEDGKSVQ GDQIKSITHF EADRHMGQAR KLLRLPKKGK KEAYLELMAK TEEENQMQVS
ENTISFPVID HAVRVDKKDQ EDNHVD