ID   RUVA_MYCAP              Reviewed;         198 AA.
AC   A5IY12;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=MAG2230;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL58921.1; -; Genomic_DNA.
DR   RefSeq; WP_011949402.1; NC_009497.1.
DR   AlphaFoldDB; A5IY12; -.
DR   SMR; A5IY12; -.
DR   STRING; 347257.MAG2230; -.
DR   EnsemblBacteria; CAL58921; CAL58921; MAG2230.
DR   KEGG; maa:MAG2230; -.
DR   HOGENOM; CLU_087936_1_1_14; -.
DR   OMA; NEYQYAT; -.
DR   Proteomes; UP000007065; Chromosome.
DR   GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro.
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   CDD; cd14332; UBA_RuvA_C; 1.
DR   HAMAP; MF_00031; DNA_helic_RuvA; 1.
DR   InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I.
DR   InterPro; IPR000085; RuvA.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR011114; RuvA_C.
DR   Pfam; PF07499; RuvA_C; 1.
DR   Pfam; PF01330; RuvA_N; 1.
DR   SUPFAM; SSF47781; SSF47781; 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..198
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT                   /id="PRO_1000090341"
SQ   SEQUENCE   198 AA;  22459 MW;  06F6033ED3F5CEBB CRC64;
     MILYRIGEII HKHNSNIIFE SQGIGYSLIL PDPERVEIKQ KCKLYLFEIK NEYQYATYAF
     KDFKERLLFV DLISLNGIGP RAAFNILNFG FEKVVALIAE GNAEALIEIP YLNPRMARLI
     VAELQAKWSK MISPKDAAKI NETTNTLSEV KETLKMVGFK TKQIDGALSK ISSTDDVEKM
     IEEAIKLMST QNYESATA