Q7UFR2 · UVRB_RHOBA
- ProteinUvrABC system protein B
- GeneuvrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids708 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | excinuclease repair complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | excinuclease ABC activity | |
Biological Process | nucleotide-excision repair | |
Biological Process | SOS response |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameUvrABC system protein B
- Short namesProtein UvrB
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Planctomycetota > Planctomycetia > Pirellulales > Pirellulaceae > Rhodopirellula
Accessions
- Primary accessionQ7UFR2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000226040 | 1-708 | UvrABC system protein B | |||
Sequence: MSITKLAPAAFDLHQPFPPSGDQPAAIAKLIEGIQSGKTAQTLLGATGTGKTYTMANVIASVQRPALILSHNKTLAAQLYGEFKEFFPNNAVHYFVSYYDYYQPEAYIPQRDVYIEKDSSINEEIDRLRLATTSSLVSRRDVVIVASVSSIYGLGSPDDYRQLVVDLHQGEQTRRDHLLLKFVDLQYQRNDIQFERGKFRVRGDSIELWPSYEEFAYRIEMWGDEIEKISLIKPTSGETIKTVEHLYIYPCKHFVMPEDRIQRAIRLLREELTQQLEIFQSQGKLLEAQRLSARTKFDLEMLAEVGHCPGIENYSRPLSGKEPGATPDTLYDFFPKDFITFVDESHVTVPQVRAMYAGDRSRKITLVEHGFRLPCALDNRPLKFDEWEERTGQICFVSATPSDYELERTGGEVVEQIIRPTGLLDPEVEIVSARGQVTHLLEQVRIRAERDERVLVTALTKRLAEDLATYFQEQGVKCRWLHSELNAFERVDLLQELRAGQFDCLVGVNLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNANSRVILYADKVTDSMQMAIDETERRRVIQMEYNAKHGIVPKTVRKSIRKGIDTEAANHKESTRKAQDSGEAIYITIEYVDKLEQEMLAAAEDLEFERAARLRDRVLQLKEHIGKPLSEVEIVDEKSAGKSGGRGRGRRGAKKKGASKGTKIPRPKRG |
Interaction
Subunit
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-419 | Helicase ATP-binding | ||||
Sequence: EGIQSGKTAQTLLGATGTGKTYTMANVIASVQRPALILSHNKTLAAQLYGEFKEFFPNNAVHYFVSYYDYYQPEAYIPQRDVYIEKDSSINEEIDRLRLATTSSLVSRRDVVIVASVSSIYGLGSPDDYRQLVVDLHQGEQTRRDHLLLKFVDLQYQRNDIQFERGKFRVRGDSIELWPSYEEFAYRIEMWGDEIEKISLIKPTSGETIKTVEHLYIYPCKHFVMPEDRIQRAIRLLREELTQQLEIFQSQGKLLEAQRLSARTKFDLEMLAEVGHCPGIENYSRPLSGKEPGATPDTLYDFFPKDFITFVDESHVTVPQVRAMYAGDRSRKITLVEHGFRLPCALDNRPLKFDEWEERTGQICFVSATPSDYELERTGGEVVEQIIR | ||||||
Motif | 98-121 | Beta-hairpin | ||||
Sequence: YYDYYQPEAYIPQRDVYIEKDSSI | ||||||
Domain | 436-598 | Helicase C-terminal | ||||
Sequence: QVTHLLEQVRIRAERDERVLVTALTKRLAEDLATYFQEQGVKCRWLHSELNAFERVDLLQELRAGQFDCLVGVNLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNANSRVILYADKVTDSMQMAIDETERRRVIQMEYNAKHGIVPKTVRKSI | ||||||
Domain | 627-662 | UVR | ||||
Sequence: IEYVDKLEQEMLAAAEDLEFERAARLRDRVLQLKEH | ||||||
Compositional bias | 668-682 | Basic and acidic residues | ||||
Sequence: SEVEIVDEKSAGKSG | ||||||
Region | 668-708 | Disordered | ||||
Sequence: SEVEIVDEKSAGKSGGRGRGRRGAKKKGASKGTKIPRPKRG | ||||||
Compositional bias | 683-708 | Basic residues | ||||
Sequence: GRGRGRRGAKKKGASKGTKIPRPKRG |
Domain
The beta-hairpin motif is involved in DNA binding.
Sequence similarities
Belongs to the UvrB family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length708
- Mass (Da)80,351
- Last updated2003-10-01 v1
- Checksum0A9DB5436BBCAABB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 668-682 | Basic and acidic residues | ||||
Sequence: SEVEIVDEKSAGKSG | ||||||
Compositional bias | 683-708 | Basic residues | ||||
Sequence: GRGRGRRGAKKKGASKGTKIPRPKRG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX294147 EMBL· GenBank· DDBJ | CAD78620.1 EMBL· GenBank· DDBJ | Genomic DNA |