Detailed information
Overview
| Name | recF | Type | Machinery gene |
| Locus tag | DR_RS05615 | Genome accession | NC_001263 |
| Coordinates | 1096951..1098030 (-) | Length | 359 a.a. |
| NCBI ID | WP_010887732.1 | Uniprot ID | Q9RVE0 |
| Organism | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 | ||
| Function | homologous recombination Homologous recombination |
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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: 1091951..1103030
| Locus tag | Gene name | Coordinates (strand) | Size (bp) | Protein ID | Product | Description |
|---|---|---|---|---|---|---|
| DR_RS05595 (DR_1085) | - | 1093053..1093808 (-) | 756 | WP_010887728.1 | class I SAM-dependent methyltransferase | - |
| DR_RS05600 (DR_1086) | alr | 1093855..1094910 (+) | 1056 | WP_027479629.1 | alanine racemase | - |
| DR_RS05605 (DR_1087) | fni | 1095075..1095959 (-) | 885 | WP_227086026.1 | type 2 isopentenyl-diphosphate Delta-isomerase | - |
| DR_RS05610 (DR_1088) | - | 1096088..1096954 (-) | 867 | WP_010887731.1 | DciA family protein | - |
| DR_RS05615 (DR_1089) | recF | 1096951..1098030 (-) | 1080 | WP_010887732.1 | DNA replication/repair protein RecF | Machinery gene |
| DR_RS05620 (DR_1090) | - | 1098196..1099266 (+) | 1071 | WP_010887733.1 | GGDEF domain-containing protein | - |
| DR_RS05625 (DR_1091) | - | 1099503..1099988 (-) | 486 | WP_010887734.1 | hypothetical protein | - |
| DR_RS05630 (DR_1092) | - | 1100063..1100557 (+) | 495 | WP_034349604.1 | hypothetical protein | - |
| DR_RS05635 (DR_1093) | trpS | 1101143..1102168 (+) | 1026 | WP_010887736.1 | tryptophan--tRNA ligase | - |
| DR_RS05640 (DR_1094) | - | 1102329..1102610 (-) | 282 | WP_034349694.1 | YiaA/YiaB family inner membrane protein | - |
| DR_RS05645 (DR_1095) | - | 1102713..1102943 (-) | 231 | WP_010887738.1 | hypothetical protein | - |
Sequence
Protein
Download Length: 359 a.a. Molecular weight: 39141.03 Da Isoelectric Point: 5.0870
MGDVRLSALSTLNYRNLAPGTLNFPEGVTGIYGENGAGKTNLLEAAYLALTGQTDAPRIEQLIQAGETEAYVRADLQQGG
SLSIQEVGLGRGRRQLKVDGVRARTGDLPRGGAVWIRPEDSELVFGPPSGRRAYLDSLLSRLSARYGEQLSRYERTVSQR
NAALRGGEEWAMHVWDDVLLKLGTEIMLFRRRALTRLDELAREANAQLGSRKTLALTLTESTSPETYAADLRGRRAEELA
RGSTVTGPHRDDLLLTLGDFPASDYASRGEGRTVALALRRAELELLREKFGEDPVLLLDDFTAELDPHRRQYLLDLAASV
PQAIVTGTELAPGAALTLRAQAGRFTPVADEEMQAEGTA
Nucleotide
Download Length: 1080 bp
ATGGGGGATGTGCGTCTCTCGGCCCTGTCTACCCTGAATTACCGGAATCTTGCGCCTGGGACGCTGAATTTCCCGGAAGG
CGTGACCGGGATTTATGGGGAGAACGGAGCTGGCAAGACCAACCTGCTCGAGGCCGCCTACCTCGCGCTGACCGGACAGA
CCGACGCGCCGCGTATCGAGCAACTGATTCAAGCGGGCGAGACCGAGGCGTATGTGCGGGCCGATTTGCAGCAGGGCGGC
AGCCTCAGCATTCAGGAAGTGGGGCTGGGGCGCGGGCGGCGGCAACTGAAGGTGGACGGCGTGCGCGCCCGGACCGGCGA
CCTGCCGCGCGGCGGAGCGGTGTGGATTCGCCCGGAAGACAGCGAACTGGTGTTCGGGCCGCCCTCGGGACGCCGGGCGT
ATCTGGACTCGCTGCTCTCGCGCCTCAGCGCCCGCTACGGCGAACAACTCTCGCGCTACGAGCGTACGGTGTCGCAGCGC
AACGCGGCCCTGCGCGGCGGCGAGGAATGGGCGATGCACGTCTGGGACGACGTCCTGCTCAAGCTCGGCACCGAAATCAT
GCTGTTTCGTCGCCGGGCGCTCACGCGGCTCGACGAACTGGCGCGCGAGGCGAACGCCCAGCTCGGCAGCCGCAAGACGC
TCGCGCTTACGCTGACCGAGAGCACCTCGCCCGAAACCTACGCCGCCGACCTGCGGGGCCGCCGCGCCGAGGAATTGGCA
CGCGGCTCCACCGTCACCGGCCCGCACCGCGACGACCTGCTGCTCACCCTGGGCGACTTTCCAGCGAGCGACTATGCCAG
CCGGGGCGAAGGCCGCACTGTCGCGCTCGCGCTGCGCCGCGCCGAACTCGAACTGCTGCGCGAGAAATTCGGCGAAGACC
CCGTTTTGCTCCTCGACGACTTCACCGCCGAACTCGACCCCCACCGCCGCCAGTACCTGCTCGACCTCGCCGCCAGCGTG
CCGCAGGCCATCGTGACCGGCACCGAACTCGCTCCCGGCGCGGCGCTGACGTTGCGGGCGCAGGCGGGGCGCTTTACTCC
AGTGGCAGATGAGGAGATGCAAGCGGAGGGCACGGCGTGA
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] | Yuan Wang et al. (2019) Distinct roles of Deinococcus radiodurans RecFOR and RecA in DNA transformation. Biochemical And Biophysical Research Communications 513(3):740-745. [PMID: 30992133] |