ADDB_STRPB
ID ADDB_STRPB Reviewed; 1071 AA.
AC Q1JCJ9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-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};
GN OrderedLocusNames=MGAS2096_Spy0657;
OS Streptococcus pyogenes serotype M12 (strain MGAS2096).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370553;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS2096;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000261; ABF35709.1; -; Genomic_DNA.
DR RefSeq; WP_002990399.1; NC_008023.1.
DR AlphaFoldDB; Q1JCJ9; -.
DR SMR; Q1JCJ9; -.
DR PRIDE; Q1JCJ9; -.
DR KEGG; spj:MGAS2096_Spy0657; -.
DR HOGENOM; CLU_007838_1_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..1071
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379402"
SQ SEQUENCE 1071 AA; 124215 MW; E1399F7FE19B938E CRC64;
MKLIYTEMSY SMTEILVNEA RKAADQGYRV FYIAPNSLSF EKEREVLTLL PERGTFSIIV
TRFVQMSRYF TVESSPSKQH LDDTTLAMIF YRALMQLKPE DLPSYGRLQN NSVFIEQLVE
LYKELKNAQL SVHDLTGLDH PQKQEDLIKI IELAETIMIQ QDYNQDSPLQ SFARAIKLGL
LNNQLSKTVI VIDGFSRFSA EEDYLLSLLN NNCQEVIIGS YVSQKAYQKS FIKGNIYEAS
LHFLQDLAQK YHIKPVFATS NQVFKPAFSR LTQLFEATHD FSQVDWQLQK NDLDHFSLWQ
CHHQKEEIEH VAKSIRQKLY EGYRYKDILV LLGDMDAYQL QIGPIFDKFE IPYYLGKAEP
MAAHPLVQFI ESLERSQRYN WRREDILNML KSGLFGCFDD SDIDRFEEYT QFADIKGFTK
FSKPFTINSS RQYPLDFLNE MRQDIVLPLQ ELFKSQKQLG ASLIDKLILF LEKIRLAENM
QGLAQSQLEV EKNEEVWKRF TDILTSFHHI FGQEKLRLSD CLALIKTGMK SAQYRVVPAT
LDVVTIKSYD LVQPHSKPFV YAIGLTQSHF PKQIHHSGLL SDQERARINE IRNYRHFDIA
SAENSKKNHQ TALSLFNAAT KELVLSVPTV INETFDDLSP YLKELINFGL PLLDKGKNYL
SYDNSDIGNY KALLSQIIAI NRQDLIEMSD QDKMFWTVVL RYLRKQLRKQ QLELPTSDYR
LSTKPLSKEV IEVCFPKGIP LKLSATALTV FYNNQYNYFL KYVLNLNKTE SIHPDSRIHG
QYLHRVFERL MKDHTQEPFD NKLKQAIYHT NQESFFQQVY QDNAEAEYSL AILEDIVRST
APILQLNQNI KVIDQEKNFH LDMGNEILVH GIIDRIDQLS DGSLGIVDYK SSANQFDIGT
FYNGLSPQLV TYLAALKQIA PHDINQLFGA MYLHLQDPKL DLVTFKQIDN TLVESIYKAL
TYKGIFSEVE KEHLSTGAYQ TKNALYSNDE LETLLNYNKY LYLKAAKHIK KGHFLINPYT
SDGKTVQGDQ LKAITRFEAD LDMAQARRLV TLPAKEKKEC FLTLMRKESH L