Detailed information
Overview
| Name | comF | Type | Machinery gene |
| Locus tag | DR_RS07135 | Genome accession | NC_001263 |
| Coordinates | 1395054..1395674 (+) | Length | 206 a.a. |
| NCBI ID | WP_027480036.1 | Uniprot ID | - |
| Organism | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 | ||
| Function | ssDNA transport into the cell DNA binding and uptake |
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Function
We identified the factors (PilQ, PilD, type IV pilins, PilB, PilT, ComEC-ComEA, and ComF) involved in DNA uptake and DNA translocation across the external and cytoplasmic membranes and showed that the DNA-uptake machinery is similar to that described in the Gram negative bacterium Vibrio cholerae.
Genomic Context
Location: 1390054..1400674
| Locus tag | Gene name | Coordinates (strand) | Size (bp) | Protein ID | Product | Description |
|---|---|---|---|---|---|---|
| DR_RS07110 (DR_1384) | - | 1390186..1390737 (-) | 552 | WP_027480035.1 | TetR/AcrR family transcriptional regulator | - |
| DR_RS07115 (DR_1385) | - | 1390917..1391408 (+) | 492 | WP_010888024.1 | DUF4142 domain-containing protein | - |
| DR_RS07120 (DR_1386) | ychF | 1391767..1392864 (+) | 1098 | WP_010888025.1 | redox-regulated ATPase YchF | - |
| DR_RS07125 (DR_1387) | - | 1392928..1394043 (-) | 1116 | WP_010888026.1 | N-acetylmuramoyl-L-alanine amidase family protein | - |
| DR_RS07130 (DR_1388) | - | 1394218..1394871 (+) | 654 | WP_010888027.1 | hypothetical protein | - |
| DR_RS07135 (DR_1389) | comF | 1395054..1395674 (+) | 621 | WP_027480036.1 | ComF family protein | Machinery gene |
| DR_RS07140 (DR_1390) | - | 1395685..1396233 (-) | 549 | WP_010888029.1 | DUF1684 domain-containing protein | - |
| DR_RS07145 (DR_1391) | - | 1396230..1396451 (-) | 222 | WP_027480037.1 | RNA-binding S4 domain-containing protein | - |
| DR_RS07150 (DR_1392) | - | 1396664..1397599 (+) | 936 | WP_027480038.1 | hypothetical protein | - |
| DR_RS07155 (DR_1393) | - | 1397656..1398369 (-) | 714 | WP_010888032.1 | histidine phosphatase family protein | - |
| DR_RS07160 (DR_1394) | purM | 1398366..1399427 (-) | 1062 | WP_162177712.1 | phosphoribosylformylglycinamidine cyclo-ligase | - |
| DR_RS07165 (DR_1395) | crtE | 1399495..1400484 (+) | 990 | WP_010888034.1 | geranylgeranyl diphosphate synthase CrtE | - |
Sequence
Protein
Download Length: 206 a.a. Molecular weight: 21651.22 Da Isoelectric Point: 10.9813
>NTDB_id=1312 DR_RS07135 WP_027480036.1 1395054..1395674(+) (comF) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
MIDLLRVLLPRACPGCGAQLGRAAGLCDRCRAELRPRVERHSPLSAQATPHLVTLGRYQGVPRRAVRALKYGGARDVAGP
LGRALAAGVPASWQIAAVVPVPLHPSRQRERGYNQAELLAQAMAAELGVPCLPLLTRTRATAQQAKLHASERSSNLAGAF
AVRGAVPPGTLLILDDVLTTGSTLLACRDALHAAGVTDLKYAAVAR
MIDLLRVLLPRACPGCGAQLGRAAGLCDRCRAELRPRVERHSPLSAQATPHLVTLGRYQGVPRRAVRALKYGGARDVAGP
LGRALAAGVPASWQIAAVVPVPLHPSRQRERGYNQAELLAQAMAAELGVPCLPLLTRTRATAQQAKLHASERSSNLAGAF
AVRGAVPPGTLLILDDVLTTGSTLLACRDALHAAGVTDLKYAAVAR
Nucleotide
Download Length: 621 bp
>NTDB_id=1312 DR_RS07135 WP_027480036.1 1395054..1395674(+) (comF) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
ATGATCGACCTGCTGCGAGTGCTGCTGCCCCGCGCCTGCCCCGGCTGCGGCGCCCAGCTGGGCCGCGCCGCCGGGCTGTG
TGACCGCTGCCGCGCGGAGCTTCGACCCCGGGTGGAGCGGCACTCGCCCCTCTCGGCGCAGGCCACGCCGCATCTGGTCA
CGCTGGGGCGGTACCAGGGCGTCCCCCGCCGGGCGGTACGGGCGCTGAAATACGGCGGGGCGCGGGACGTGGCCGGGCCG
CTGGGGCGGGCGCTCGCAGCGGGGGTTCCGGCGAGCTGGCAAATAGCCGCTGTGGTGCCGGTGCCGCTGCATCCTTCGCG
CCAGCGTGAGCGCGGGTACAACCAGGCCGAGTTGCTGGCGCAGGCGATGGCCGCTGAGCTGGGGGTGCCTTGCCTGCCGC
TCCTCACCCGCACCCGCGCCACCGCTCAGCAGGCCAAGTTGCACGCCAGCGAGCGCAGCAGCAATCTGGCGGGGGCTTTC
GCGGTGCGCGGCGCCGTGCCGCCAGGCACCCTCCTCATTCTGGACGATGTGCTGACGACCGGCAGCACGCTCCTGGCCTG
CCGGGACGCCCTGCACGCGGCGGGCGTGACCGACCTGAAATACGCGGCGGTAGCGCGCTAA
ATGATCGACCTGCTGCGAGTGCTGCTGCCCCGCGCCTGCCCCGGCTGCGGCGCCCAGCTGGGCCGCGCCGCCGGGCTGTG
TGACCGCTGCCGCGCGGAGCTTCGACCCCGGGTGGAGCGGCACTCGCCCCTCTCGGCGCAGGCCACGCCGCATCTGGTCA
CGCTGGGGCGGTACCAGGGCGTCCCCCGCCGGGCGGTACGGGCGCTGAAATACGGCGGGGCGCGGGACGTGGCCGGGCCG
CTGGGGCGGGCGCTCGCAGCGGGGGTTCCGGCGAGCTGGCAAATAGCCGCTGTGGTGCCGGTGCCGCTGCATCCTTCGCG
CCAGCGTGAGCGCGGGTACAACCAGGCCGAGTTGCTGGCGCAGGCGATGGCCGCTGAGCTGGGGGTGCCTTGCCTGCCGC
TCCTCACCCGCACCCGCGCCACCGCTCAGCAGGCCAAGTTGCACGCCAGCGAGCGCAGCAGCAATCTGGCGGGGGCTTTC
GCGGTGCGCGGCGCCGTGCCGCCAGGCACCCTCCTCATTCTGGACGATGTGCTGACGACCGGCAGCACGCTCCTGGCCTG
CCGGGACGCCCTGCACGCGGCGGGCGTGACCGACCTGAAATACGCGGCGGTAGCGCGCTAA
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] |