ADDB_STRA5
ID ADDB_STRA5 Reviewed; 1077 AA.
AC Q8E062;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=SAG0873;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99759.1; -; Genomic_DNA.
DR RefSeq; NP_687887.1; NC_004116.1.
DR RefSeq; WP_000772298.1; NC_004116.1.
DR AlphaFoldDB; Q8E062; -.
DR SMR; Q8E062; -.
DR STRING; 208435.SAG0873; -.
DR EnsemblBacteria; AAM99759; AAM99759; SAG0873.
DR KEGG; sag:SAG0873; -.
DR PATRIC; fig|208435.3.peg.880; -.
DR HOGENOM; CLU_007838_1_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000000821; 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 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; Reference proteome.
FT CHAIN 1..1077
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379389"
SQ SEQUENCE 1077 AA; 124020 MW; B2C803A76476E038 CRC64;
MKLLYTDINH DMTEILVNQA AHAAEAGWRI FYIAPNSLSF EKERAVLENL PQEASFAITI
TRFAQLARYF TLNQPNQKES LNDIGLAMIF YRALASFEDG QLKVFGRLKQ DASFISQLVD
LYKELQTANL SILELKYLHS PEKFEDLLAI FLVVSDLLRE GEYDNQSKIA FFTEQVRSGQ
LDVDLKNTIL IVDGFTRFSA EEEALIKSLS SRCQEIIIGA YASQKAYKAN FTNGNIYSAG
VDFLRYLATT FQTKPEFILS KWESKSGFEM ISKNIEGKHD FTNSSHILDD TAKDCITIWE
CINQKDEVEH VARAIRQKLY QGYRYKDILV LLGDVDSYKL QLSKIFEQYD IPYYFGKAET
MAAHPLVHFM DSLSRIKRYR FRAEDVLNLF KTGIYGEISQ DDLDYFEAYI SYADIKGPKK
FFTDFVVGAK KFDLGRLNTI RQSLLTPLES FVKTKKQDGI KTLNQFMFFL TQVGLSDNLS
RLVGQMSENE QEKHQEVWKT FTDILEQFQT IFGQEKLNLD EFLSLLNSGM MQAEYRMVPA
TVDVVTVKSY DLVEPHSNQF VYALGMTQSH FPKIAQNKSL ISDIERQLIN DANDTDGHFD
IMTQENLKKN HFAALSLFNA AKQELVLTIP QLLNESEDQM SPYLVELRDI GVPFNHKGRQ
SLKEEADNIG NYKALLSRVV DLYRSAIDKE MTKEEQTFWS VAVRYLRRQL TSKGIEIPII
TDSLDTVTVS SDVMTRRFPE DDPLKLSSSA LTTFYNNQYK YFLQYVLGLE EQDSIHPDMR
HHGTYLHRVF EILMKNQGIE SFEEKLNSAI NKTNQEDVFK SLYSEDAESR YSLEILEDIA
RATATILRQD SQMTVESEEE RFELMIDNTI KINGIIDRID RLSDGSLGVV DYKSSAQKFD
IQKFYNGLSP QLVTYIDAIS RDKEVEQKPP IFGAMYLHMQ EPRQDLSKIK NLDDLVTKNH
QALTYKGLFS EAEKEFLANG KYHLKDSLYS ETEIAILQAH NQSLYKKASE TIKSGKFLIN
PYTEDAKTVD GDQFKSITGF EADRHMARAR ALYKLPAKEK RQGFLTLMQQ EEENDDL