Detailed information    

experimental Experimentally validated

Overview


Name   comEC   Type   Machinery gene
Locus tag   DR_RS09490 Genome accession   NC_001263
Coordinates   1877260..1879527 (-) Length   755 a.a.
NCBI ID   WP_010888489.1    Uniprot ID   -
Organism   Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539     
Function   ssDNA transport through the inner membrane   
DNA binding and uptake

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: 1872260..1884527
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  DR_RS09470 (DR_1849) msrA 1873832..1874404 (+) 573 WP_051618834.1 peptide-methionine (S)-S-oxide reductase MsrA -
  DR_RS09475 (DR_1850) - 1874404..1874631 (+) 228 WP_010888485.1 hypothetical protein -
  DR_RS09480 (DR_1851) - 1874710..1875465 (-) 756 WP_010888486.1 serine/threonine-protein kinase -
  DR_RS09485 (DR_1852) - 1875540..1876553 (-) 1014 WP_034350037.1 SIS domain-containing protein -
  DR_RS09490 (DR_1854) comEC 1877260..1879527 (-) 2268 WP_010888489.1 DNA internalization-related competence protein ComEC/Rec2 Machinery gene
  DR_RS09495 (DR_1855) comEA 1879521..1879901 (-) 381 WP_010888490.1 ComEA family DNA-binding protein Machinery gene
  DR_RS09505 (DR_1856) gatA 1880131..1881579 (+) 1449 WP_010888491.1 Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatA -
  DR_RS09510 (DR_1857) - 1881637..1882056 (-) 420 WP_010888492.1 organic hydroperoxide resistance protein -
  DR_RS09515 (DR_1858) - 1882162..1882914 (+) 753 WP_010888493.1 TSUP family transporter -
  DR_RS09520 (DR_1859) - 1882952..1883563 (-) 612 WP_010888494.1 hypothetical protein -
  DR_RS09525 (DR_1860) - 1883538..1883735 (-) 198 WP_164927979.1 DUF4388 domain-containing protein -
  DR_RS09530 (DR_1861) scpB 1883839..1884387 (-) 549 WP_010888496.1 SMC-Scp complex subunit ScpB -

Sequence


Protein


Download         Length: 755 a.a.        Molecular weight: 79381.05 Da        Isoelectric Point: 10.8771

>NTDB_id=1311 DR_RS09490 WP_010888489.1 1877260..1879527(-) (comEC) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
MVTREGATRFDPQTGEVLTAPARRRGHRAEAGRLAWPLPLALGIIGGIGWQLGLGWAAVPLLLGAALALLDARPLLAVLA
LLGGGLGYGSAHLQAREPDRIAPWIGALVTLRGHWDGQFLTLDEPKARVALAPKPRQGPGEVVVAGRLIRPDGRRIPGGF
DQAAWLRSQGGLLVPTPKAVLVRAEVKKHVPERGLRGWFRRGLSAHLSPRNAALMTAVELGERGDIGRETFDEGFSVRDA
FARAGLAHLMALSGQNVALLTGTLIWLLGWLGARPSWRYGLPAALLPFYLLLLVGATPSITRAVLMGGVALLALMVGRGR
PDPLGIVALTASACLLLFPLWLLDVGFQLSFLAVLGLLLSGKLADRLPQRWPQWLKLALAATVLAELATLPVIAHNFGQL
PLVGLPANLLAAPIMAVLVPLGFLAGLLGPAGGLVNWAVAPLASALLWVAQTFGSAPVLGWGTLGAGGFLAYALAAVAGM
GWLLGRVRGQAALTIALACAALSWLPAQLRPARELVFLDVGQGDATLLRVPGLTMLVDGGGSVGSDYDVGRGTVLPALRA
LGVRKLDVVVATHADTDHIEGLSSVLRGLPVGELWVGQLKKAGDDPVLDAVLTAARERNVPVRQIRRGDQVTAGPVKVTA
LWPVGNVWSTADNDNSVALRVEDGPFRAALLGDLPDPAEALIGPGHLTLLKAAHHGSRYSTGEVLLKQTKPKDVLISVGR
NTYGHPTQAVLDRIAAAGAKVWRTDQVGTVRWPLP

Nucleotide


Download         Length: 2268 bp        

>NTDB_id=1311 DR_RS09490 WP_010888489.1 1877260..1879527(-) (comEC) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
ATGGTGACTCGTGAAGGGGCGACCCGCTTCGACCCGCAAACGGGTGAGGTGCTGACTGCCCCTGCCCGCCGTCGGGGTCA
CCGCGCCGAGGCCGGGCGGCTGGCGTGGCCGCTCCCCCTCGCGCTCGGCATCATCGGCGGCATCGGGTGGCAGCTCGGGC
TGGGGTGGGCCGCCGTGCCGCTGCTGCTCGGTGCAGCGTTGGCCCTGCTGGACGCCCGCCCGCTGCTGGCGGTGCTCGCG
CTGCTCGGTGGAGGACTGGGGTACGGCTCGGCGCACTTGCAGGCCCGCGAGCCGGACCGCATCGCCCCCTGGATAGGTGC
CCTCGTGACCCTGCGCGGCCACTGGGACGGGCAATTTCTGACGCTGGACGAGCCGAAAGCGCGGGTGGCCCTCGCTCCCA
AACCGAGGCAAGGGCCGGGCGAAGTGGTGGTGGCCGGGCGGCTGATTCGCCCCGATGGCCGGCGTATTCCCGGCGGCTTT
GACCAGGCGGCGTGGCTGCGCTCGCAAGGCGGGCTTCTGGTGCCCACGCCGAAAGCCGTGCTGGTGCGTGCCGAGGTCAA
AAAGCATGTCCCGGAACGTGGCCTGCGCGGCTGGTTTCGTCGGGGCCTGAGTGCCCATCTCTCGCCCCGCAACGCTGCCC
TGATGACGGCGGTGGAACTCGGCGAGCGCGGTGACATCGGACGCGAAACGTTTGATGAGGGCTTCTCGGTGCGCGACGCC
TTTGCCCGCGCTGGGCTCGCGCACCTGATGGCGTTGAGCGGGCAGAACGTGGCGCTGCTGACTGGCACATTGATCTGGCT
GCTCGGGTGGCTGGGGGCGCGGCCCAGCTGGCGCTATGGCCTGCCCGCCGCGCTGCTGCCCTTTTACCTGCTGCTCCTCG
TCGGCGCCACACCGAGCATCACCCGCGCCGTGCTGATGGGCGGTGTGGCCCTGCTCGCGCTGATGGTGGGCCGGGGGCGG
CCCGACCCGTTGGGCATCGTGGCGCTGACAGCGAGTGCCTGCCTGCTGTTGTTTCCGCTGTGGCTGCTGGACGTGGGGTT
TCAGCTTTCCTTTCTGGCGGTCCTCGGCCTGCTGCTCTCGGGCAAACTGGCCGACCGGCTGCCGCAGCGCTGGCCGCAGT
GGCTCAAGCTCGCGCTCGCGGCCACCGTGCTCGCCGAACTCGCCACCCTGCCAGTCATCGCGCACAATTTCGGGCAACTG
CCGCTGGTGGGCTTGCCCGCCAACCTGCTCGCCGCGCCCATCATGGCGGTGCTGGTGCCGCTCGGCTTCCTCGCGGGGCT
GCTCGGCCCGGCAGGCGGGCTGGTGAACTGGGCCGTGGCGCCGCTCGCTTCTGCTCTGCTGTGGGTCGCGCAGACTTTCG
GCAGTGCCCCGGTGCTGGGCTGGGGCACGCTCGGCGCGGGCGGCTTTCTTGCCTACGCGCTCGCCGCTGTTGCGGGGATG
GGTTGGCTGCTCGGGCGGGTGCGGGGGCAAGCCGCGTTGACCATTGCCCTCGCCTGCGCCGCGCTGTCCTGGCTGCCGGC
CCAGTTGCGCCCCGCCCGCGAACTGGTCTTTCTGGACGTGGGCCAGGGCGACGCCACCCTGCTGCGGGTGCCGGGCCTGA
CGATGCTCGTGGACGGCGGCGGCTCGGTCGGCAGCGACTACGACGTGGGCCGGGGCACCGTGTTGCCGGCTTTGCGGGCT
CTCGGGGTGCGGAAGCTGGACGTGGTGGTGGCGACGCACGCCGACACCGACCACATCGAGGGCCTTTCCAGCGTCCTGCG
CGGTCTTCCGGTGGGCGAGTTGTGGGTGGGCCAGCTCAAAAAGGCGGGCGACGACCCGGTGCTCGACGCCGTGCTGACCG
CTGCCCGTGAAAGAAATGTCCCGGTGCGCCAGATTCGGCGGGGCGACCAGGTGACGGCGGGACCGGTCAAAGTGACGGCT
CTGTGGCCTGTCGGCAACGTCTGGTCCACTGCTGACAACGACAACTCGGTGGCGCTGCGGGTCGAGGACGGACCATTCCG
TGCCGCCTTGCTCGGTGACTTGCCCGACCCCGCCGAGGCCCTGATTGGCCCCGGTCACCTCACGCTGCTCAAGGCCGCGC
ACCACGGCAGCCGCTACAGCACCGGCGAAGTCCTCCTCAAGCAGACGAAGCCGAAAGACGTGCTTATCAGCGTGGGACGC
AACACTTACGGACACCCGACACAGGCGGTGCTCGACCGAATAGCCGCTGCCGGGGCGAAGGTATGGCGGACCGATCAGGT
GGGAACGGTGCGGTGGCCTTTGCCTTGA


Secondary structure


Protein secondary structures were predicted by S4PRED and visualized by seqviz.



3D structure


Source ID Structure

Transmembrane helices


Transmembrane helices of protein were predicted by TMHMM 2.0 and visualized by seqviz and ECharts.



Visualization of predicted probability:


Similar proteins


Only experimentally validated proteins are listed.

Protein Organism Identities (%) Coverage (%) Ha-value
  comA/comEC Thermus thermophilus HB27

40.85

90.399

0.369


Multiple sequence alignment    



References


[1] Dhirendra Kumar Sharma et al. (2025) Surviving the storm: exploring the role of natural transformation in nutrition and DNA repair of stressed Deinococcus radiodurans. Applied And Environmental Microbiology 91(1):e0137124. [PMID: 39651863]
[2] 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]