Detailed information    

experimental Experimentally validated

Overview


Name   dprA   Type   Machinery gene
Locus tag   DR_RS00625 Genome accession   NC_001263
Coordinates   118232..119344 (-) Length   370 a.a.
NCBI ID   WP_010886768.1    Uniprot ID   -
Organism   Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539     
Function   ssDNA binding; loading RecA onto ssDNA   
DNA processing

Function


DrDprA can function as a recombination mediator through RecA loading onto ssDNA in vivo, as described in other bacteria.


Genomic Context


Location: 113232..124344
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  DR_RS17040 (DR_0115) - 114210..114995 (+) 786 WP_164927943.1 S-layer homology domain-containing protein -
  DR_RS16565 (DR_0116) - 114929..115282 (+) 354 WP_234944658.1 hypothetical protein -
  DR_RS00610 (DR_0117) accC 115396..116733 (-) 1338 WP_010886765.1 acetyl-CoA carboxylase biotin carboxylase subunit -
  DR_RS00615 (DR_0118) accB 116822..117385 (-) 564 WP_010886766.1 acetyl-CoA carboxylase biotin carboxyl carrier protein -
  DR_RS00620 (DR_0119) efp 117584..118141 (-) 558 WP_010886767.1 elongation factor P -
  DR_RS00625 (DR_0120) dprA 118232..119344 (-) 1113 WP_010886768.1 DNA-processing protein DprA Machinery gene
  DR_RS00630 (DR_0121) - 119580..120743 (-) 1164 WP_027480301.1 tetratricopeptide repeat protein -
  DR_RS00635 (DR_0122) - 120888..121730 (+) 843 WP_027480300.1 metalloenzyme domain protein -
  DR_RS00640 (DR_0123) - 121944..122570 (-) 627 WP_010886771.1 phosphoribosylanthranilate isomerase -
  DR_RS00645 (DR_0124) - 122563..122847 (-) 285 WP_010886772.1 hypothetical protein -
  DR_RS00650 (DR_0125) - 122858..123373 (-) 516 WP_010886773.1 GNAT family N-acetyltransferase -

Sequence


Protein


Download         Length: 370 a.a.        Molecular weight: 37775.19 Da        Isoelectric Point: 6.6652

>NTDB_id=1314 DR_RS00625 WP_010886768.1 118232..119344(-) (dprA) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
MTLPSPAAAHAELLALLTLRFTPGLGPRRIENLRRHFGSAEAALAAPLTELRRVEGLDSRSVAAIGGAKAAEEARAELNK
AAERGVTLLGRGLPGYPAALEALGDPPAVLWVRGAGGAELLAGLGTVPHSVGIVGTRAASPHALALTRTIAGELAAAGVL
IVSGLARGVDTAAHTAALEAASGEASSPTIGVLGSAVDVIYPRENHDLAGRMVVVSEYPLGTGPAQHHFPSRNRVIAALS
AGVLVVEGERKSGSLITATHALDCGRTVFAVPGRAGDPRASGPHALIRDGAVLTESAQDVLTELNWGLAPAPAVPDLPPE
QARVLRALQTPATLDDLAATTGLSIPELQTALVMLQLQGLAYEVGGRWSR

Nucleotide


Download         Length: 1113 bp        

>NTDB_id=1314 DR_RS00625 WP_010886768.1 118232..119344(-) (dprA) [Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539]
GTGACCCTTCCCTCCCCTGCTGCCGCCCACGCCGAACTGCTGGCCCTGCTCACCCTGCGGTTTACGCCCGGACTGGGGCC
ACGGCGCATCGAAAACCTGCGGCGGCATTTCGGCAGCGCGGAGGCGGCACTGGCGGCGCCTCTGACCGAGCTGCGGCGGG
TGGAGGGGCTGGACTCGCGTTCGGTGGCGGCGATTGGCGGGGCAAAAGCGGCAGAGGAGGCGCGGGCCGAACTGAACAAG
GCGGCAGAGCGCGGCGTCACCCTGCTCGGACGCGGTTTGCCCGGCTATCCGGCGGCGCTGGAAGCCCTGGGTGATCCGCC
CGCCGTGCTGTGGGTGCGGGGCGCGGGCGGCGCCGAGCTGCTCGCCGGGCTCGGCACCGTGCCGCACTCGGTGGGCATCG
TGGGCACGCGGGCAGCGAGTCCCCACGCGCTGGCGCTGACCCGGACCATCGCAGGCGAGCTGGCAGCAGCAGGCGTCCTC
ATCGTCAGCGGGCTGGCGCGGGGGGTGGACACGGCGGCGCACACGGCAGCCCTGGAAGCTGCAAGCGGGGAGGCGAGCAG
CCCCACCATCGGGGTGCTCGGCAGCGCGGTGGACGTGATTTATCCGCGTGAAAACCATGACCTCGCCGGGCGAATGGTGG
TCGTCAGCGAGTATCCGCTCGGCACCGGCCCGGCGCAGCACCACTTCCCGAGCCGCAACCGCGTCATCGCCGCGCTCTCG
GCGGGCGTGCTGGTGGTGGAAGGCGAGCGCAAGTCCGGTTCGCTCATCACCGCTACTCACGCGCTGGACTGCGGGCGCAC
CGTGTTCGCCGTGCCGGGGCGGGCCGGCGACCCCCGCGCGAGTGGCCCCCACGCCCTGATTCGTGACGGGGCTGTCCTCA
CCGAGTCGGCGCAGGACGTGCTGACCGAGCTGAACTGGGGCCTGGCCCCTGCCCCAGCGGTGCCCGACCTGCCGCCCGAG
CAAGCGCGGGTGCTGCGGGCGCTGCAAACCCCGGCCACATTGGACGACCTTGCCGCCACAACTGGCCTGAGCATTCCCGA
GTTGCAGACCGCGCTCGTCATGTTGCAGCTTCAGGGGCTGGCCTACGAAGTGGGCGGGCGTTGGAGTCGCTGA


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
  dprA Thermus thermophilus HB27

45.392

87.725

0.398


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] Dhirendra Kumar Sharma et al. (2024) Natural transformation-specific DprA coordinate DNA double-strand break repair pathways in heavily irradiated D. radiodurans. Applied And Environmental Microbiology 90(2):e0194823. [PMID: 38193676]
[3] Dhirendra Kumar Sharma et al. (2022) Characterization of DNA Processing Protein A (DprA) of the Radiation-Resistant Bacterium Deinococcus radiodurans. Microbiology Spectrum 10(6):e0347022. [PMID: 36453941]
[4] 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]