RUVA_BORBU
ID RUVA_BORBU Reviewed; 197 AA.
AC P70827; O51054;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031};
GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; OrderedLocusNames=BB_0023;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-197.
RC STRAIN=HB19;
RX PubMed=9766225; DOI=10.1016/s0923-2508(98)80299-4;
RA Boursaux-Eude C., Margarita D., Belfaiza J., Old I.G., Saint-Girons I.;
RT "Homologues of helicase genes priA and ruvAB of Borrelia burgdorferi, the
RT Lyme borreliosis agent.";
RL Res. Microbiol. 149:235-245(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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. RuvA stimulates,
CC in the presence of DNA, the weak ATPase activity of RuvB.
CC {ECO:0000255|HAMAP-Rule:MF_00031}.
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_00031};
CC -!- SUBUNIT: Forms a complex with RuvB. {ECO:0000255|HAMAP-Rule:MF_00031}.
CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP-
CC Rule:MF_00031}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y08885; CAA70096.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66409.1; -; Genomic_DNA.
DR PIR; G70102; G70102.
DR RefSeq; NP_212157.1; NC_001318.1.
DR RefSeq; WP_002658353.1; NC_001318.1.
DR AlphaFoldDB; P70827; -.
DR SMR; P70827; -.
DR STRING; 224326.BB_0023; -.
DR EnsemblBacteria; AAC66409; AAC66409; BB_0023.
DR GeneID; 56568192; -.
DR KEGG; bbu:BB_0023; -.
DR PATRIC; fig|224326.49.peg.422; -.
DR HOGENOM; CLU_087936_2_0_12; -.
DR OMA; VGMAVQC; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 2.40.50.140; -; 1.
DR HAMAP; MF_00031; DNA_helic_RuvA; 1.
DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000085; RuvA.
DR InterPro; IPR010994; RuvA_2-like.
DR Pfam; PF01330; RuvA_N; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00084; ruvA; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..197
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_0000094606"
FT CONFLICT 103
FT /note="K -> R (in Ref. 1; CAA70096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 22688 MW; A652BEF96DACA30C CRC64;
MINKIHGKVI EKKESSLVLM TTVFEFELLV SAFCLANFNL SDKVELFTYL YTRENELKLF
GFLNSDEREI FKELIGVSGV GPRAALRVLS NIRYNEFKEA IDKEDIELVS KIKGIGKKMA
GKMFLHLQGK LLINSELEST GLFRFKELEE SIVSMGFDRK IVNSKIREAF NLAEFANLKD
SEKEQFLFKE VLKRISN