RUVB_THETH
ID RUVB_THETH Reviewed; 324 AA.
AC Q56214; Q9RA64;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016};
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8626340; DOI=10.1128/jb.178.9.2695-2700.1996;
RA Tong J., Wetmur J.G.;
RT "Cloning, sequencing, and expression of ruvB and characterization of RuvB
RT proteins from two distantly related thermophilic eubacteria.";
RL J. Bacteriol. 178:2695-2700(1996).
CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC cruciform structure in supercoiled DNA with palindromic sequence,
CC indicating that it may promote strand exchange reactions in homologous
CC recombination. RuvAB is a helicase that mediates the Holliday junction
CC migration by localized denaturation and reannealing. RuvB is a Mg(2+)-
CC dependent, DNA-dependent ATPase with an equal preference for
CC supercoiled and linear duplex DNA. It can promote Holliday junction
CC migration alone.
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_00016};
CC -!- ACTIVITY REGULATION: The activity of RuvB is enhanced by RuvA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:8626340};
CC -!- SUBUNIT: Forms a complex with RuvA.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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DR EMBL; U22817; AAB03726.2; -; Genomic_DNA.
DR PIR; T11851; T11851.
DR AlphaFoldDB; Q56214; -.
DR SMR; Q56214; -.
DR DIP; DIP-41108N; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00016; DNA_helic_RuvB; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041445; AAA_lid_4.
DR InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008824; RuvB-like_N.
DR InterPro; IPR008823; RuvB_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR42848; PTHR42848; 1.
DR Pfam; PF17864; AAA_lid_4; 1.
DR Pfam; PF05491; RuvB_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00635; ruvB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; Helicase;
KW Hydrolase; Nucleotide-binding; SOS response.
FT CHAIN 1..324
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000165620"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ SEQUENCE 324 AA; 36016 MW; 1B0DB92F373185CE CRC64;
MEDLALRPKT LDEYIGQERL KQKLRVYLEA AKARKEPLEH LLLFGPPGLG KTTLAHVIAH
ELGVNLRVTS GPAIEKPGDL AAILANSLEE GDILFIDEIH RLSRQAEEHL YPAMEDFVMD
IVIGQGPAAR TIRLELPRFA LIGATTRPGL ITAPLLSRFG IVEHLEYYTP EELAQGVMRD
ARLLGVRITE EAALEIGRRS RGTMRVAKRL FRRVRDFAQV EGEEVITRER ALEALAALGL
DELGLEKRDR EILEVLILRF GAGPVGLATL ATALSEDPGT LEEVHEPYLI RQGLLKRTPR
GRVATELAYR HLGYPPPVGP LLEP