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RUVA_RHOBA
ID   RUVA_RHOBA              Reviewed;         207 AA.
AC   Q7USB0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=RB4610;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294140; CAD73887.1; -; Genomic_DNA.
DR   RefSeq; NP_866201.1; NC_005027.1.
DR   RefSeq; WP_007326966.1; NC_005027.1.
DR   AlphaFoldDB; Q7USB0; -.
DR   SMR; Q7USB0; -.
DR   STRING; 243090.RB4610; -.
DR   EnsemblBacteria; CAD73887; CAD73887; RB4610.
DR   KEGG; rba:RB4610; -.
DR   PATRIC; fig|243090.15.peg.2161; -.
DR   eggNOG; COG0632; Bacteria.
DR   HOGENOM; CLU_087936_3_0_0; -.
DR   InParanoid; Q7USB0; -.
DR   OMA; MITRITA; -.
DR   OrthoDB; 1370858at2; -.
DR   Proteomes; UP000001025; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000085; RuvA.
DR   InterPro; IPR010994; RuvA_2-like.
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..207
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT                   /id="PRO_1000195174"
SQ   SEQUENCE   207 AA;  22713 MW;  0158DFABBAE02595 CRC64;
     MIVSIAGKLV QVGEISVIIQ AAPFDYEVYV GDYTRRQLQN QIGNEVRLHT LDYIEGNAQG
     GRLTPRLIGF STLPERQFFD LFCSVDGVGV KKALRAMVRP VKELAVLIEE QDAKTLSALP
     GIGPATSEKV IAKLRRKMPR FALMVAGGEV ADAMEVESPI VSDTYDALVT LGHSESDARK
     LIDETLATGK KFKDTESLLT AIYQRSK
 
 
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