Detailed information    

experimental Experimentally validated

Overview

Name   comEA   Type   Machinery gene
Locus tag   DR_RS09495 Genome accession   NC_001263
Coordinates   1879521..1879901 (-) Length   126 a.a.
NCBI ID   WP_010888490.1    Uniprot ID   Q9RTB0
Organism   Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539     
Function   dsDNA binding   
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: 1874521..1884901
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  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: 126 a.a.        Molecular weight: 13354.65 Da        Isoelectric Point: 10.7165

>NTDB_id=1310 DR_RS09495 WP_010888490.1 1879521..1879901(-) (comEA) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
MLPHERLWQVALAAGALLVGGLTLGPALLPRPQLPTVTRTALPPVQADANAEPRTYPTTASVTPLISGRVNLNTASQEQL
EALPKVGPAMAKKIIAGRPYHSLADLDRVKGVGEATLRTLTPLVKW

Nucleotide


Download         Length: 381 bp        

>NTDB_id=1310 DR_RS09495 WP_010888490.1 1879521..1879901(-) (comEA) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
ATGCTCCCTCACGAACGGCTCTGGCAGGTGGCGCTGGCGGCGGGCGCTTTGCTCGTCGGCGGCCTGACCCTCGGCCCCGC
GCTGCTGCCGCGCCCGCAGCTGCCGACGGTGACGCGCACGGCGCTGCCGCCCGTTCAGGCCGACGCGAACGCCGAGCCGC
GGACTTACCCGACCACTGCGAGCGTCACGCCCCTCATCAGCGGGCGGGTGAACCTGAACACGGCGAGTCAGGAGCAGCTC
GAAGCCCTTCCCAAAGTCGGCCCGGCGATGGCGAAGAAAATTATCGCCGGGCGGCCCTACCACTCGCTCGCTGACCTGGA
CCGCGTGAAAGGCGTGGGCGAAGCGACCCTCCGCACGCTGACGCCGCTGGTGAAATGGTGA

Domains

Predicted by InterproScan.

Helix-hairpin-helix motif (HHH_3)

(69-123)


Secondary structure

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



3D structure

Source ID Structure
  AlphaFold DB Q9RTB0

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
  comEA Thermus thermophilus HB27

39.815

100

0.422

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]