ID   RUVB_GEOSM              Reviewed;         337 AA.
AC   C6E1S8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN   Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; OrderedLocusNames=GM21_0930;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00016}.
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_00016};
CC   -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00016}.
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DR   EMBL; CP001661; ACT16997.1; -; Genomic_DNA.
DR   RefSeq; WP_012774612.1; NC_012918.1.
DR   AlphaFoldDB; C6E1S8; -.
DR   SMR; C6E1S8; -.
DR   STRING; 443144.GM21_0930; -.
DR   EnsemblBacteria; ACT16997; ACT16997; GM21_0930.
DR   KEGG; gem:GM21_0930; -.
DR   eggNOG; COG2255; Bacteria.
DR   HOGENOM; CLU_055599_1_0_7; -.
DR   OMA; IHRMSRP; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00016; DNA_helic_RuvB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041445; AAA_lid_4.
DR   InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008824; RuvB-like_N.
DR   InterPro; IPR008823; RuvB_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR42848; PTHR42848; 1.
DR   Pfam; PF17864; AAA_lid_4; 1.
DR   Pfam; PF05491; RuvB_C; 1.
DR   Pfam; PF05496; RuvB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00635; ruvB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; Helicase;
KW   Hydrolase; Nucleotide-binding; SOS response.
FT   CHAIN           1..337
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT                   /id="PRO_1000201837"
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   337 AA;  36775 MW;  073DDAA3847A1957 CRC64;
     MTRLISADKS EDDLLEASLR PRALSDYVGQ EKAKGNLGLF IDAARGRGEA LDHVLLYGPP
     GLGKTTLANI IACEMGVNIK STSGPVIERP GDLAAILTNL EAHDVLFIDE IHRLSHVVEE
     ILYPAMEDFQ LDIIIGQGPS ARTIKLDLPK FTLVGATTRA GLLSSPLRDR FGVISRLEFY
     THDELAFIIT RSARIFGMAI APEGAMELAR RSRGTPRIAN RLLRRVRDFA QVRADGVITR
     AVADQALALL EIDEMGFDMM DRAILLTIID KFGGGPVGLD TIAAAISEES DTIEDVYEPF
     LIQNGFLNRT PRGRVATAAA YSHFGRIAPE PPQGKLF