P9WGW1 · RUVB_MYCTU

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). RuvB binds Holliday junction (HJ) DNA in the presence of RuvA (PubMed:22094465).
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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site24ATP (UniProtKB | ChEBI)
Binding site25ATP (UniProtKB | ChEBI)
Binding site66ATP (UniProtKB | ChEBI)
Binding site69ATP (UniProtKB | ChEBI)
Binding site70ATP (UniProtKB | ChEBI)
Binding site70Mg2+ (UniProtKB | ChEBI)
Binding site71ATP (UniProtKB | ChEBI)
Binding site132-134ATP (UniProtKB | ChEBI)
Binding site175ATP (UniProtKB | ChEBI)
Binding site185ATP (UniProtKB | ChEBI)
Binding site222ATP (UniProtKB | ChEBI)
Binding site314DNA (UniProtKB | ChEBI)
Binding site319DNA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentHolliday junction resolvase complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionfour-way junction DNA binding
Molecular Functionfour-way junction helicase activity
Biological ProcessDNA recombination
Biological ProcessDNA repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Holliday junction branch migration complex subunit RuvB
  • EC number

Gene names

    • Name
      ruvB
    • ORF names
      MTCY227.09
    • Ordered locus names
      Rv2592c

Organism names

Accessions

  • Primary accession
    P9WGW1
  • Secondary accessions
    • L0TCV1
    • P66753
    • Q50629

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001655621-344Holliday junction branch migration complex subunit RuvB

Proteomic databases

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.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-185Large ATPase domain (RuvB-L)
Region186-256Small ATPAse domain (RuvB-S)
Region259-344Head 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 status
    Complete
  • Length
    344
  • Mass (Da)
    36,627
  • Last updated
    2014-04-16 v1
  • Checksum
    5C12036B1FDE89F9
MTERSDRDVSPALTVGEGDIDVSLRPRSLREFIGQPRVREQLQLVIEGAKNRGGTPDHILLSGPPGLGKTSLAMIIAAELGSSLRVTSGPALERAGDLAAMLSNLVEHDVLFIDEIHRIARPAEEMLYLAMEDFRVDVVVGKGPGATSIPLEVAPFTLVGATTRSGALTGPLRDRFGFTAHMDFYEPAELERVLARSAGILGIELGADAGAEIARRSRGTPRIANRLLRRVRDFAEVRADGVITRDVAKAALEVYDVDELGLDRLDRAVLSALTRSFGGGPVGVSTLAVAVGEEAATVEEVCEPFLVRAGMVARTPRGRVATALAWTHLGMTPPVGASQPGLFE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP45388.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp