Detailed information
Overview
| Name | ddrB | Type | Machinery gene |
| Locus tag | DR_RS00370 | Genome accession | NC_001263 |
| Coordinates | 66037..66603 (+) | Length | 188 a.a. |
| NCBI ID | WP_027480237.1 | Uniprot ID | - |
| Organism | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 | ||
| Function | DNA binding DNA binding and uptake |
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Function
The transformation frequency of the cells devoid of DprA, a highly conserved protein among competent species, strongly decreased but was not completely abolished whereas it was completely abolished in ΔdprA ΔrecF, ΔdprA ΔrecO, and ΔdprA ΔddrB double mutants. We propose that RecF and RecO, belonging to the recombination mediator complex, and DdrB, a specific deinococcal DNA binding protein, can replace a function played by DprA, or alternatively, act at a different step of recombination with DprA.
Genomic Context
Location: 61037..71603
| Locus tag | Gene name | Coordinates (strand) | Size (bp) | Protein ID | Product | Description |
|---|---|---|---|---|---|---|
| DR_RS00350 (DR_0066) | - | 63356..64144 (-) | 789 | WP_027480238.1 | APH(3') family aminoglycoside O-phosphotransferase | - |
| DR_RS00355 (DR_0067) | - | 64184..65113 (+) | 930 | WP_010886715.1 | hypothetical protein | - |
| DR_RS00360 (DR_0068) | - | 65110..65484 (+) | 375 | WP_010886716.1 | hypothetical protein | - |
| DR_RS00365 (DR_0069) | - | 65586..65948 (+) | 363 | WP_010886717.1 | hypothetical protein | - |
| DR_RS00370 (DR_0070) | ddrB | 66037..66603 (+) | 567 | WP_027480237.1 | single-stranded DNA-binding protein DdrB | Machinery gene |
| DR_RS00375 (DR_0071) | - | 66759..68720 (-) | 1962 | WP_234944657.1 | peptidylprolyl isomerase | - |
| DR_RS00385 (DR_0072) | - | 69092..69571 (+) | 480 | WP_027480236.1 | hypothetical protein | - |
Sequence
Protein
Download Length: 188 a.a. Molecular weight: 20830.32 Da Isoelectric Point: 9.2754
MLQIEFITDLGARVTVNVEHESRLLDVQRHYGRLGWTSGEIPSGGYQFPIENEADFDWSLIGARKWKSPEGEELVIHRGH
AYRRRELEAVDSRKLKLPAAIKYSRGAKVSDPQHVREKADGDIEYVSLAIFRGGKRQERYAVPGGAAGNGQGRPAPQGQP
AQARPQATAARPAARPPVQPGQEEETPF
Nucleotide
Download Length: 567 bp
ATGTTGCAGATTGAATTTATCACCGACCTGGGTGCGCGGGTCACGGTGAACGTGGAGCATGAAAGCCGGTTGCTGGACGT
ACAGCGCCACTATGGCCGCCTGGGCTGGACCAGCGGCGAGATTCCGTCCGGGGGCTACCAGTTTCCCATCGAGAACGAGG
CCGACTTCGACTGGTCGCTGATCGGCGCCCGCAAGTGGAAGAGCCCCGAGGGCGAAGAACTCGTCATTCACCGGGGCCAC
GCCTACCGCCGCCGCGAACTCGAAGCCGTGGACAGCCGCAAGCTCAAGCTGCCTGCCGCCATCAAGTACAGCCGCGGCGC
CAAGGTCAGCGACCCGCAGCACGTGCGCGAAAAGGCCGATGGCGACATCGAATACGTCAGCCTCGCCATCTTCCGCGGTG
GCAAGCGGCAGGAGCGCTACGCGGTGCCCGGCGGCGCGGCGGGGAACGGTCAGGGTCGCCCGGCGCCCCAGGGACAGCCC
GCCCAGGCCCGTCCCCAGGCCACTGCCGCTCGCCCCGCCGCTCGGCCCCCGGTGCAGCCCGGTCAGGAAGAAGAAACGCC
GTTCTGA
3D structure
| Source | ID | Structure |
|---|
Similar proteins
Only experimentally validated proteins are listed.
| Protein | Organism | Identities (%) | Coverage (%) | Ha-value |
|---|
References
| [1] | Solenne Ithurbide et al. (2020) Natural Transformation in Deinococcus radiodurans: A Genetic Analysis Reveals the Major Roles of DprA, DdrB, RecA, RecF, and RecO Proteins. Frontiers in Microbiology 11:1253. [PMID: 32625182] |
| [2] | Claire Bouthier de la Tour et al. (2011) The deinococcal DdrB protein is involved in an early step of DNA double strand break repair and in plasmid transformation through its single-strand annealing activity. DNA Repair 10(12):1223-31. [PMID: 21968057] |