Q1YLZ8 · Q1YLZ8_AURMS
- ProteinUvrABC system protein B
- GeneuvrB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1102 (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 | |
Molecular Function | helicase activity | |
Biological Process | nucleotide-excision repair | |
Biological Process | SOS response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUvrABC system protein B
- Short namesProtein UvrB
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Aurantimonadaceae > Aurantimonas
Accessions
- Primary accessionQ1YLZ8
Proteomes
Subcellular Location
Interaction
Subunit
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-126 | Disordered | ||||
Sequence: MASRSRTTRSRPASDTAEDEAPFDPGAPARRGGFAEAPQADFEAAREFAGPVSGWADEIAQGLETTAEHVADGDNPAPAAAEPEPAKAKAKPAAKSSKAAASTGARPGKTSRGTSMGGTSDPKQRA | ||||||
Compositional bias | 103-121 | Polar residues | ||||
Sequence: TGARPGKTSRGTSMGGTSD | ||||||
Domain | 213-361 | Helicase ATP-binding | ||||
Sequence: SGITDHDQTQVLLGVTGSGKTFSVANVIERTQRPALILAPNKTLAAQLYGEFKNFFPDNAVEYFVSYYDYYQPEAYVPRSDTFIEKESSINEQIDRMRHAATRALLERDDVIIVASVSCIYGIGSVETYTAMTFQMSIGDRLDQRQLLA | ||||||
Motif | 279-302 | Beta-hairpin | ||||
Sequence: YYDYYQPEAYVPRSDTFIEKESSI | ||||||
Coiled coil | 444-471 | |||||
Sequence: NQAVRLIKEELRHRLVELEKAGRLLEAQ | ||||||
Domain | 618-784 | Helicase C-terminal | ||||
Sequence: QVDDLVGEIRDTVDKGYRVLATVLTKRMAEDLTEYLHEQGIRVRYMHSDIDTLERIEIIRDLRLGAFDVLVGINLLREGLDIPECGLVAILDADKEGFLRSETSLIQTIGRAARNIDGKVILYADRTTGSMERAIAETNRRREKQEAYNAEHGITPASVKAQIADIL | ||||||
Coiled coil | 808-835 | |||||
Sequence: GNNLKSHLEHLEKQMRDAAADLDFETAA | ||||||
Domain | 812-847 | UVR | ||||
Sequence: KSHLEHLEKQMRDAAADLDFETAARLRDEIKRLQAK | ||||||
Region | 850-871 | Disordered | ||||
Sequence: EFGGLPGGDSGSGGKKARGGGN | ||||||
Region | 892-1102 | Disordered | ||||
Sequence: PVTGRSKYGRKTKRDRQPAGGERFGPRGEPLKPRGEGSDRRPAPLARPPRPGDAAASPAGHDASAPSDGASGQHGGDTAAGSYFQKPSLDDMGPGTDTARPDRPGLFRKNSLDEMTVGRTEKPVGKPAPKKPAPRKPADTASPKADTGSGTGPGMGKSTNTNAPHGEPVEPRTSSDDAAPIRRERIGRGSYEDPTDQKRKRRPGKTGRPGR | ||||||
Compositional bias | 904-934 | Basic and acidic residues | ||||
Sequence: KRDRQPAGGERFGPRGEPLKPRGEGSDRRPA | ||||||
Compositional bias | 993-1019 | Basic and acidic residues | ||||
Sequence: DRPGLFRKNSLDEMTVGRTEKPVGKPA | ||||||
Compositional bias | 1035-1059 | Polar residues | ||||
Sequence: KADTGSGTGPGMGKSTNTNAPHGEP | ||||||
Compositional bias | 1061-1091 | Basic and acidic residues | ||||
Sequence: EPRTSSDDAAPIRRERIGRGSYEDPTDQKRK |
Domain
The beta-hairpin motif is involved in DNA binding.
Sequence similarities
Belongs to the UvrB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,102
- Mass (Da)119,932
- Last updated2006-05-02 v1
- Checksum0048FF0745B33C2C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 103-121 | Polar residues | ||||
Sequence: TGARPGKTSRGTSMGGTSD | ||||||
Compositional bias | 904-934 | Basic and acidic residues | ||||
Sequence: KRDRQPAGGERFGPRGEPLKPRGEGSDRRPA | ||||||
Compositional bias | 993-1019 | Basic and acidic residues | ||||
Sequence: DRPGLFRKNSLDEMTVGRTEKPVGKPA | ||||||
Compositional bias | 1035-1059 | Polar residues | ||||
Sequence: KADTGSGTGPGMGKSTNTNAPHGEP | ||||||
Compositional bias | 1061-1091 | Basic and acidic residues | ||||
Sequence: EPRTSSDDAAPIRRERIGRGSYEDPTDQKRK |
Keywords
- Technical term