ADDB_STRPM
ID ADDB_STRPM Reviewed; 1071 AA.
AC Q48UB9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=M28_Spy0573;
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180;
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA Lefebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(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; CP000056; AAX71687.1; -; Genomic_DNA.
DR RefSeq; WP_011284663.1; NC_007296.2.
DR AlphaFoldDB; Q48UB9; -.
DR SMR; Q48UB9; -.
DR EnsemblBacteria; AAX71687; AAX71687; M28_Spy0573.
DR KEGG; spb:M28_Spy0573; -.
DR HOGENOM; CLU_007838_1_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000009292; 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.
FT CHAIN 1..1071
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379406"
SQ SEQUENCE 1071 AA; 124207 MW; 834515C7D0B9ED2F 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 ASLVDKLILF FKKIRLAENM
QGLAQSQLEV EKNEEVWKRF TDILTSFHHI FGQEKLRLSD CLALIKTGMK SAQYRVVPAT
LDVVTIKSYD LVQPHSKPFV YAIGLTQSHF PKQIHHSGLL SDQERARINE IRNYRHFDIA
SAENSKKNHQ TALSLFNAAT KELVLSVPTV INETFDDLSP YLKELISFGL 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