A0A1E9JHX0 · A0A1E9JHX0_9FUSO
- ProteinHolliday junction branch migration complex subunit RuvB
- GeneruvB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids340 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 20 | ATP (UniProtKB | ChEBI) | |||
Binding site | 21 | ATP (UniProtKB | ChEBI) | |||
Binding site | 62 | ATP (UniProtKB | ChEBI) | |||
Binding site | 65 | ATP (UniProtKB | ChEBI) | |||
Binding site | 66 | ATP (UniProtKB | ChEBI) | |||
Binding site | 66 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 67 | ATP (UniProtKB | ChEBI) | |||
Binding site | 171 | ATP (UniProtKB | ChEBI) | |||
Binding site | 181 | ATP (UniProtKB | ChEBI) | |||
Binding site | 218 | ATP (UniProtKB | ChEBI) | |||
Binding site | 310 | DNA (UniProtKB | ChEBI) | |||
Binding site | 315 | DNA (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | Holliday junction resolvase complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | four-way junction DNA binding | |
Molecular Function | four-way junction helicase activity | |
Biological Process | DNA recombination | |
Biological Process | DNA repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHolliday junction branch migration complex subunit RuvB
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Fusobacteriota > Fusobacteriia > Fusobacteriales > Fusobacteriaceae > Fusobacterium
Accessions
- Primary accessionA0A1E9JHX0
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer. Forms an RuvA8-RuvB12-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA4-RuvB12-RuvC2 complex forms which resolves the HJ.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-181 | Large ATPase domain (RuvB-L) | |||
Domain | 51-179 | AAA+ ATPase | |||
Region | 182-252 | Small ATPAse domain (RuvB-S) | |||
Region | 255-340 | Head domain (RuvB-H) | |||
Domain
Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Sequence similarities
Belongs to the RuvB family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length340
- Mass (Da)37,725
- Last updated2017-02-15 v1
- Checksum61BE39FDE75242AC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LTHT01000066 EMBL· GenBank· DDBJ | OFL90843.1 EMBL· GenBank· DDBJ | Genomic DNA |