ID A0A1B9ARL2_9BACI Unreviewed; 333 AA. AC A0A1B9ARL2; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 28-JUN-2023, entry version 27. 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=A8L44_08985 {ECO:0000313|EMBL:OCA86524.1}; OS Bacillus sp. FJAT-27986. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA86524.1, ECO:0000313|Proteomes:UP000092673}; RN [1] {ECO:0000313|EMBL:OCA86524.1, ECO:0000313|Proteomes:UP000092673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA86524.1, RC ECO:0000313|Proteomes:UP000092673}; RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J., RA Liu B., Liu G.; RT "Bacillus sp. FJAT-27986."; RL Submitted (MAY-2016) 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:OCA86524.1}. 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; MAYV01000014; OCA86524.1; -; Genomic_DNA. DR RefSeq; WP_066105481.1; NZ_MAYV01000014.1. DR AlphaFoldDB; A0A1B9ARL2; -. DR STRING; 1743146.A8L44_08985; -. DR EnsemblBacteria; OCA86524; OCA86524; A8L44_08985. DR OrthoDB; 9804478at2; -. DR Proteomes; UP000092673; 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_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; -; 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. DR TIGRFAMs; TIGR00635; ruvB; 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:OCA86524.1}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000092673}. FT DOMAIN 52..183 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 2..182 FT /note="Large ATPase domain (RuvB-L)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT REGION 183..253 FT /note="Small ATPAse domain (RuvB-S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT REGION 256..333 FT /note="Head domain (RuvB-H)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 63 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 66 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 67 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 129..131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 311 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" FT BINDING 316 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016" SQ SEQUENCE 333 AA; 37174 MW; 711CDB90DD9B22EF CRC64; MEERIMDLHA QNQDETFEYS LRPHSLEQYI GQDKVKENLR VFIEAAKMRE EALDHVLLYG PPGLGKTTLA TIIANEMGVE IRTTSGPAIE RPGDLAAILS SLQPGEVLFI DEIHRLPKSV EEVLYPAMED FCLDIVIGKG PGARSVRLDL PPFTLVGATT RAGALSAPLR DRFGVISRLE YYTESQLREI VTRTAQVLDT AIEESAASEI ARRSRGTPRI ANRLLRRVRD FAQVRGDGDI QFGLADYALE LMQVDKVGLD QIDRKLLLGI IEKFKGGPVG LDTIAATIGE ESGTIEDVYE PYLMQIGFMQ RTPRGRIVTE HVYRHFNLEV PNS //