ADDB_STRP1
ID ADDB_STRP1 Reviewed; 1071 AA.
AC Q9A0H4; Q48ZK6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=SPy_0776, M5005_Spy0594;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK33716.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51212.1; -; Genomic_DNA.
DR RefSeq; NP_268995.1; NC_002737.2.
DR AlphaFoldDB; Q9A0H4; -.
DR SMR; Q9A0H4; -.
DR STRING; 1314.HKU360_00605; -.
DR PaxDb; Q9A0H4; -.
DR EnsemblBacteria; AAK33716; AAK33716; SPy_0776.
DR KEGG; spy:SPy_0776; -.
DR KEGG; spz:M5005_Spy0594; -.
DR PATRIC; fig|160490.10.peg.662; -.
DR HOGENOM; CLU_007838_1_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000000750; 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; -; 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; Reference proteome.
FT CHAIN 1..1071
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379401"
FT CONFLICT 142
FT /note="Q -> K (in Ref. 2; AAZ51212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1071 AA; 124158 MW; 8D4F455B9891C9CF CRC64;
MKLIYTEMSY SMTEILVNEA RKAADQGYRV FYIAPNSLSF EKEREVLTLL PERGTFSIIV
TRFVQMSRYF TVESSPSKQH LDDTTLAMIF YRALMQLKPE DLPSYGRLQN NSVFIEQLVE
LYKELKNAQL SVHDLTGLDH PQKQEDLIKI IELAETIMIQ QDYNQDSPLQ SFARAIKLGL
LNNQLSKTVV VIDGFSRFSA EEDYLLSLLN NNCQEVIIGS YVSQKAYQKS FIKGNIYEAS
LHFLQDLAQK YHIKPVFATS NQVFKPAFSR LTQLFEATHD FSQVDWQLQK SDLDHFSLWQ
CHHQKEEIEH VAKSIRQKLY EGYRYKDILV LLGDMDAYQL QIGPIFDKFE IPYYLGKAEP
MAAHPLVQFI ESLERSQRYN WRREDILNML KSGLFGCFDD SDIDRFEEYT QFADIKGFTK
FSKPFTINSS RQYPLDFLNE MRQDIVLPLQ ELFKSQKQLG ASLVDKLILF LKKIRLAENM
QGLAQSQLEV EKNEEVWKRF TDILTSFHHI FGQEKLRLSD CLALIKTGMK SAQYRVVPAT
LDVVTIKSYD LVQPHSKPFV YAIGLTQSHF PKQIHHSGLL SDQERARINE IRNYRHFDIA
SAENSKKNHQ TALSLFNAAT KELVLSVSTV INETFDDLSP YLKELINFGL PLLDKGKNYL
SYDNSDIGNY KALLSQIIAI NRQDLIEMSD QDKMFWTVVL RYLRKQLRKQ QLELPTSDYR
LSTKPLSKEV IEVCFPKGIP LKLSATALTV FYNNQYNYFL KYVLNLNKTE SIHPDSRIHG
QYLHRVFERL MKDHTQEPFD NKLKQAIYHT NQESFFQQVY QDNAEAEYSL AILEDIVRST
APILQLNQNI QVIDQEKNFQ LDMGNEILVH GIIDRIDQLS DGSLGIVDYK SSANQFDIGT
FYNGLSPQLM TYLAALKQIA PHDINQLFGA MYLHLQDPKL DLVTFKQIDN TLVESIYKAL
TYKGIFSEVE KEHLSTGAYQ TKNALYSNDE LETLLNYNKY LYLKAAKHIK KGHFLINPYT
SDGKTVQGDQ LKAITRFEAD LDMGQARRLV TLPAKEKKEC FLTLMRKESH L
