A0A1G2MJH3 · A0A1G2MJH3_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.

167650100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site41-48ATP (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
      A3D50_01525

Organism names

Accessions

  • Primary accession
    A0A1G2MJH3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain28-186Helicase ATP-binding
Motif94-117Beta-hairpin
Domain443-609Helicase C-terminal
Domain636-671UVR

Domain

The beta-hairpin motif is involved in DNA binding.

Sequence similarities

Belongs to the UvrB family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    676
  • Mass (Da)
    76,165
  • Last updated
    2017-02-15 v1
  • MD5 Checksum
    DBCBC3519955FEC8649756561C95B4FD
MKTKSIFKLSSSFKPAGDQIKAIASLRQGLSKNIQHQTLLGVTGSGKTFTMANIIADYGKPTLVIAHNKTLAAQLAQEYKEFFPHNAVHYFVSYYDYYQPEAYIPATDTYIEKEAMINEEIDRLRHASTQALLTRNDVIIVASVSCIYGLGSPAEYQKVNLKISTGSELSRAEIIRQLVNIHFKRTTADLKPGDFRALGNTVEIMPVNDKTVYRLEYDGGHIGNIIEIDPVSRTLRGNHQTVFIFPAKHFMSNADQVSQAVETIQDELSDRLKVLQKSGKILEAERLKRRVRYDLAMIREIGYTNGIENYSRHFSGMTPGQPPDTLLSYFPKTKEGKPDFLTIIDESHVTVPQLRGMYAGDASRKETLVEHGFRLPSAKDNRPLKFDEFMERVGPLIYTSATPSDYEKGISGQIVEQVIRPTGLVDPEIVVRPITPKISYLGQIADFIIEVEKAVSKGDRALATTLTKKMAEDLSEYLKEKGIKASYLHSDIKTMERITILTEFRKGKYDCLVGVNLLREGLDLPEVSLIGILDADKEGFLRSDTALIQTVGRAARNIAGRVILYADNITGSIKRAIEETSRRRSIQLSYNKAHHITPKTIVKHIKDITDQIRSDRDRAVDELVKIDDELARTNPKRLVREKEKAMSDAVKELDFETAAIIRDELIVLKKKYDIVQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MHRM01000013
EMBL· GenBank· DDBJ
OHA24023.1
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.
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