ID A0A0A2WM79_THEFI Unreviewed; 321 AA. AC A0A0A2WM79; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 13-SEP-2023, entry version 33. DE RecName: Full=Holliday junction branch migration complex subunit RuvB {ECO:0000256|HAMAP-Rule:MF_00016}; DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_00016}; GN Name=ruvB {ECO:0000256|HAMAP-Rule:MF_00016}; GN ORFNames=THFILI_03480 {ECO:0000313|EMBL:KGQ20923.1}; OS Thermus filiformis. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ20923.1, ECO:0000313|Proteomes:UP000030364}; RN [1] {ECO:0000313|EMBL:KGQ20923.1, ECO:0000313|Proteomes:UP000030364} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ20923.1, RC ECO:0000313|Proteomes:UP000030364}; RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I., RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.; RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280 RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) CC DNA during genetic recombination and DNA repair, while the RuvA-RuvB CC complex plays an important role in the rescue of blocked DNA CC replication forks via replication fork reversal (RFR). RuvA CC specifically binds to HJ cruciform DNA, conferring on it an open CC structure. The RuvB hexamer acts as an ATP-dependent pump, pulling CC dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on CC either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per CC hexamer contact DNA at a time. Coordinated motions by a converter CC formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and CC nucleotide exchange. Immobilization of the converter enables RuvB to CC convert the ATP-contained energy into a lever motion, pulling 2 CC nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus CC driving DNA branch migration. The RuvB motors rotate together with the CC DNA substrate, which together with the progressing nucleotide cycle CC form the mechanistic basis for DNA recombination by continuous HJ CC branch migration. Branch migration allows RuvC to scan DNA until it CC finds its consensus sequence, where it cleaves and resolves cruciform CC DNA. {ECO:0000256|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:0000256|ARBA:ARBA00001665, ECO:0000256|HAMAP- CC Rule:MF_00016}; CC -!- SUBUNIT: Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) CC complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters CC through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA CC strand where it exits the tetramer. Each RuvB hexamer is contacted by CC two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this CC complex drives branch migration. In the full resolvosome a probable CC DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ. CC {ECO:0000256|HAMAP-Rule:MF_00016}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00016}. CC -!- DOMAIN: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) CC domains and the C-terminal head (RuvB-H) domain. The head domain binds CC DNA, while the ATPase domains jointly bind ATP, ADP or are empty CC depending on the state of the subunit in the translocation cycle. CC During a single DNA translocation step the structure of each domain CC remains the same, but their relative positions change. CC {ECO:0000256|HAMAP-Rule:MF_00016}. CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|HAMAP- CC Rule:MF_00016}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00016}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KGQ20923.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JPSL02000037; KGQ20923.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0A2WM79; -. DR STRING; 276.THFILI_03480; -. DR EnsemblBacteria; KGQ20923; KGQ20923; THFILI_03480. DR PATRIC; fig|276.5.peg.2298; -. DR OrthoDB; 9804478at2; -. DR Proteomes; UP000030364; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0000400; F:four-way junction DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR CDD; cd00009; AAA; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR HAMAP; MF_00016; DNA_HJ_migration_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 NCBIfam; TIGR00635; ruvB; 1. DR PANTHER; PTHR42848; -; 1. DR PANTHER; PTHR42848:SF1; HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE RUVB; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00016}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00016}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00016}; Helicase {ECO:0000313|EMBL:KGQ20923.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00016}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00016}. FT DOMAIN 36..168 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 168..238 FT /note="Small ATPAse domain (RuvB-S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT REGION 241..321 FT /note="Head domain (RuvB-H)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 5 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 6 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 47 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 51 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 52 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 114..116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 157 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 296 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 301 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" SQ SEQUENCE 321 AA; 35849 MW; ED15CF062B47F245 CRC64; MEPALRPKTL DEYVGQERLK KKLRVYLEAA KARKEPLDHL LLVGPPGLGK TTLAHIIAYE LGVKIRVTSG PAIEKPGDLA AILTNSLDEG DVLFIDEIHR LSRQAEEHLY PAMEDFKMDI VIGQGPAART LRLDLPRFTL IGATTRPGLL TSPLRSRFGI VEHLEFYTVE ELAQAIRRDA ALLGLEVEEE AAQEMGRRSR GTMRIAKRLF RRVRDFAEVA GERRITLERT LEALRALGLD ELGLEKRDRE ILETLILRFG GGPVGLVTLA TALAEDPGTL EEVYEPYLIQ LGLLKRTPRG RVATEAAYRH LGFALPMDPL L //