A0A8J4WNQ1 · A0A8J4WNQ1_9BACT

Function

function

The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA2B2 complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Features

Showing features for binding site.

1759100200300400500600700
TypeIDPosition(s)Description
Binding site37-44ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentexcinuclease repair complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular Functionexcinuclease ABC activity
Biological Processnucleotide-excision repair
Biological ProcessSOS response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    UvrABC system protein B
  • Short names
    Protein UvrB
  • Alternative names
    • Excinuclease ABC subunit B

Gene names

    • Name
      uvrB
    • ORF names
      Udaeo2_19440

Organism names

  • Taxonomic identifier
  • Strain
    • AEW3
  • Taxonomic lineage
    Bacteria > Verrucomicrobiota > Spartobacteria > Chthoniobacterales > Chthoniobacteraceae > Candidatus Udaeobacter

Accessions

  • Primary accession
    A0A8J4WNQ1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.

Family & Domains

Features

Showing features for domain, motif, coiled coil, region, compositional bias.

Type
IDPosition(s)Description
Domain24-158Helicase ATP-binding
Motif90-113Beta-hairpin
Coiled coil251-289
Region434-474Disordered
Compositional bias443-473Basic and acidic residues
Domain505-671Helicase C-terminal
Domain695-730UVR
Region731-759Disordered
Compositional bias745-759Basic residues

Domain

The beta-hairpin motif is involved in DNA binding.

Sequence similarities

Belongs to the UvrB family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    759
  • Mass (Da)
    86,268
  • Last updated
    2022-05-25 v1
  • Checksum
    AB5BDFBF1EF580A9
MSFQLQSNYTPRGDQGQAIAKLIRSIEAGNRHQTLLGVTGSGKTFTIANVIRELDRPTLVISHNKTLAAQLYSEFKQFFPRNAVEYFVSYFDYYQPEAYIPRSDTYIEKDSSINEEIERLRLAATSALLSRRDTIVVASVSCIYGVTSPEDYLQMLLTIKRGQQVSREAVLSRLIEMLYDRNDVNFARGRFRVRGDVVEVYPGSADEEGIRIEFFGDEIEAITRFDPLTGHAHESLSVITFYPAKQFVTPADKLNRALRTIRDELEERIIELESQNKLLEAQRLRMRTEYDLEMLQEMGFCNGIENYSRHLSGRPPGSKPYTIIDFFPKDFLVVIDESHATIPQIGGMYEGDRSRKTVLVNYGFRLPSALDNRPLNFDEFMKLTNQLVYVSATPAEFEIQNSVAGNKGYIPHRRQRIGEAELVPFAVAGEKRSTPINREQALNSDKSRARAQRSRSNSEVRVSRTDEPPEKFDVHTPGAQLVVEQIIRPTGLLDPKITLKPLKNQIDETIELCRQRVEKGERVLVTTLTKRTAEDLADYLRDVGLKVRYLHSDIDAIERVEILRGLRAADFDILVGINLLREGLDLPEVSLVCILDADKEGFLRSETSLIQTAGRAARHVNGEVVLFADQVTRSMEALMSISEYRRAKQLEYNEKHGITPQTVRRAVQESLHTILRGREIAASVIQEAGGDFNVTELLRELEDEMQEASANLEFERAALLRDQIMEVKSGTGISKIEPKRRPVKYSSRGRGTGRRRSRV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias443-473Basic and acidic residues
Compositional bias745-759Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAALOD010000047
EMBL· GenBank· DDBJ
KAF5407919.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help