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RUVA_GLUOX
ID   RUVA_GLUOX              Reviewed;         200 AA.
AC   Q5FQC5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=GOX1681;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW61421.1; -; Genomic_DNA.
DR   RefSeq; WP_011253203.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FQC5; -.
DR   SMR; Q5FQC5; -.
DR   STRING; 290633.GOX1681; -.
DR   EnsemblBacteria; AAW61421; AAW61421; GOX1681.
DR   KEGG; gox:GOX1681; -.
DR   eggNOG; COG0632; Bacteria.
DR   HOGENOM; CLU_087936_3_0_5; -.
DR   OMA; VGMAVQC; -.
DR   Proteomes; UP000006375; 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   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   InterPro; IPR011114; RuvA_C.
DR   InterPro; IPR036267; RuvA_C_sf.
DR   Pfam; PF07499; RuvA_C; 1.
DR   Pfam; PF01330; RuvA_N; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF46929; SSF46929; 1.
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..200
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT                   /id="PRO_0000224872"
SQ   SEQUENCE   200 AA;  20875 MW;  B746ECD1BBAF13AB CRC64;
     MIGQLTGLVG QIEGERCIVD VNGVGYVVSA STRTLAVLPQ PPSVARVLIE TIVREDAIQL
     FGFATTDERD WFRLLTTVQS VGAKVALAIL SANNPGELLL AINAGDKGSL TRAAGVGPRL
     ADRILSELRN KVAKMPGGGG TVSAPGIVSG PSVENDALLA LAGLGFRRAE AWPVLSKVLA
     ENENATLDLA IRLSLKDLAR
 
 
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