RUVA_TREPA
ID RUVA_TREPA Reviewed; 227 AA.
AC O83554;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
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=TP_0543;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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}.
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DR EMBL; AE000520; AAC65527.1; -; Genomic_DNA.
DR PIR; D71312; D71312.
DR RefSeq; WP_010881990.1; NC_021490.2.
DR AlphaFoldDB; O83554; -.
DR SMR; O83554; -.
DR IntAct; O83554; 1.
DR STRING; 243276.TPANIC_0543; -.
DR EnsemblBacteria; AAC65527; AAC65527; TP_0543.
DR GeneID; 57879067; -.
DR KEGG; tpa:TP_0543; -.
DR eggNOG; COG0632; Bacteria.
DR HOGENOM; CLU_087936_2_0_12; -.
DR OMA; VGMAVQC; -.
DR OrthoDB; 1370858at2; -.
DR Proteomes; UP000000811; 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..227
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_0000094703"
SQ SEQUENCE 227 AA; 24399 MW; 6B66933517D37156 CRC64;
MFESISGILT LHERERLCVE VHGIEWEIAV SAYSSAAFGE VGSHVKVFTW LYHREDALRL
FGFSNVQERT LFLSLTKVEG IGPKQALKVL SSISSQALCA ALDTGDLCAL QRIPGIGKKT
AQRMLLALKG TLALTDAASC AQSQTDDRAA HPSNLGCAPH AREIEDLVTA LVQMGYDRKM
AAEVIAQESA ALCSVGRSLY EEEATVLKRA ILALSIAHPH AVAPAAE