ADDB_STRPQ
ID ADDB_STRPQ Reviewed; 1071 AA.
AC P0CZ55; Q79WR0; Q8K816;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 53.
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=SPs1341;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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; BA000034; BAC64436.1; -; Genomic_DNA.
DR RefSeq; WP_011054337.1; NC_004606.1.
DR AlphaFoldDB; P0CZ55; -.
DR SMR; P0CZ55; -.
DR PRIDE; P0CZ55; -.
DR KEGG; sps:SPs1341; -.
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_0000411265"
SQ SEQUENCE 1071 AA; 124333 MW; 7AD18F20EB1A778E 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 NDLDHFSLWQ
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 KELVLSVPTV INETFDDLSP YLKELINFGL PLLDKGKNYL
SYDNSDIGNY KALLSQIIAI NRQDLIEMSD QDKMFWTVVL RYLRKQLRKQ QLELPTSDYR
LSTKSLSKEV IEVCFPKRIP LKLSATALTV FYNNQYNYFL KYVLNLNKTE SIHPDSRIHG
QYLHRVFERL MKDHTQEPFD NKLKQAIYHT NQESFFQQIY QDNAEAEYSL AILEDIVRST
APILQLNQNI QVIDQEKNFH LDMGNEILVH GIIDRIDQLS DGSLGIVDYK SSANQFDIGT
FYNGLSPQLV TYLAALKQIT PHDINQLFGA MYLHLQDPKL DLVTFKQIDN TLVESIYKAL
TYKGIFSEVE KEHLSTGAYQ TKNALYSNDE LETLLNYNRY LYLKAAKHIK KGHFLINPYT
SDGKTVQGDQ LKAITRFEAD LDMGQARRLV TLPAKEKKEC FLTLMRKESH L