Detailed information    

experimental Experimentally validated

Overview

Name   dprA   Type   Machinery gene
Locus tag   BSU_16110 Genome accession   NC_000964
Coordinates   1682580..1683473 (+) Length   297 a.a.
NCBI ID   NP_389493.1    Uniprot ID   P39813
Organism   Bacillus subtilis subsp. subtilis str. 168     
Function   ssDNA binding; loading RecA onto ssDNA   
DNA processing

Function

DprA is essential for efficient chromosomal and plasmid transformation. It interacts with ssDNA-binding proteins (SSBs) such as SsbA and SsbB, facilitating the displacement of these proteins and allowing RecA to nucleate onto ssDNA.


Genomic Context

Location: 1677580..1688473
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  BSU_16070 (BSU16070) ylqG 1678250..1679980 (+) 1731 NP_389489.1 putative glycosyltransferase -
  BSU_16080 (BSU16080) ylqH 1679977..1680258 (+) 282 NP_389490.1 putative flagellar biosynthesis protein -
  BSU_16090 (BSU16090) sucC 1680431..1681588 (+) 1158 NP_389491.1 succinyl-CoA synthetase (beta subunit) -
  BSU_16100 (BSU16100) sucD 1681617..1682519 (+) 903 NP_389492.1 succinyl-CoA synthetase (alpha subunit) -
  BSU_16110 (BSU16110) dprA 1682580..1683473 (+) 894 NP_389493.1 DNA processing Smf single strand binding protein Machinery gene
  BSU_16120 (BSU16120) topA 1683661..1685736 (+) 2076 NP_389494.1 DNA topoisomerase I -
  BSU_16130 (BSU16130) trmFO 1685812..1687119 (+) 1308 NP_389495.1 tRNA:m(5)U-54 methyltransferase -
  BSU_16140 (BSU16140) codV 1687187..1688101 (+) 915 NP_389496.1 site-specific tyrosine recombinase for chromosome partitioning -

Sequence

Protein


Download         Length: 297 a.a.        Molecular weight: 32935.26 Da        Isoelectric Point: 9.9142

>NTDB_id=114 BSU_16110 NP_389493.1 1682580..1683473(+) (dprA) [Bacillus subtilis subsp. subtilis str. 168]
MDQAAVCLTICRINQLLSPSLLLKWWKADPSMSLTSPVLQTVTRDQIKAAALKNEIEQFYPKLPRVLAAYREQGINTIPI
SSKQYPFWLKSIYDPPAVLFAKGDMTLLSKGRKIGIVGTRNPTAYGKQVVNHLTKEICRKGWVIVSGLASGIDGMSHAAS
IKAKGRTIGVIAGGFQHIYPRENLQLADHMAKHHILLSEHPPETKPQKWHFPMRNRIISGLSEGVIVVQGKEKSGSLITA
YQALEQGREVFAVPGSLFDPYAGGPIKLIQQGAKAIWSAEDIFEELPERNVQYTEPF

Nucleotide


Download         Length: 894 bp        

>NTDB_id=114 BSU_16110 NP_389493.1 1682580..1683473(+) (dprA) [Bacillus subtilis subsp. subtilis str. 168]
TTGGATCAGGCCGCTGTCTGCCTAACGATTTGCAGAATCAATCAATTATTATCCCCATCCCTTCTATTAAAATGGTGGAA
AGCCGATCCGTCTATGTCGCTGACATCACCCGTGTTACAAACGGTTACTCGTGATCAAATAAAAGCAGCTGCATTAAAAA
ACGAAATAGAACAATTTTATCCAAAGCTCCCGCGTGTACTTGCTGCTTATCGTGAGCAAGGCATTAACACCATCCCTATT
TCTTCAAAGCAATATCCTTTCTGGCTTAAAAGCATTTATGATCCCCCTGCCGTACTGTTTGCAAAAGGTGATATGACTCT
TCTTTCGAAAGGGAGAAAAATTGGAATTGTAGGCACAAGAAATCCAACAGCTTATGGGAAACAAGTTGTCAATCATCTTA
CAAAAGAGATCTGTCGTAAAGGTTGGGTGATTGTCAGCGGACTGGCGTCTGGGATAGACGGAATGTCCCATGCTGCAAGT
ATTAAGGCGAAGGGGCGGACAATTGGCGTCATTGCAGGCGGATTTCAACACATTTATCCCCGAGAAAACCTTCAGTTAGC
AGATCACATGGCTAAACACCATATCCTGCTGTCAGAGCACCCACCTGAAACTAAACCCCAAAAATGGCATTTCCCTATGA
GAAACCGTATTATCAGCGGACTAAGTGAAGGCGTTATTGTCGTTCAGGGCAAAGAAAAAAGCGGTTCGCTGATTACTGCC
TATCAAGCATTGGAACAAGGGAGAGAGGTATTTGCCGTACCCGGTTCATTGTTTGACCCTTACGCCGGAGGTCCTATAAA
ACTGATCCAGCAGGGGGCTAAAGCCATATGGTCAGCAGAGGATATTTTCGAGGAACTTCCTGAGAGAAACGTTCAATATA
CGGAACCCTTTTGA

Domains

Predicted by InterproScan.

DNA recombination-mediator protein A (DNA_processg_A)

(71-276)


Secondary structure

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



3D structure

Source ID Structure
  AlphaFold DB P39813

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 Lactococcus lactis subsp. cremoris KW2

42.105

94.326

0.397
  dprA Legionella pneumophila strain ERS1305867

38.462

100

0.387

Multiple sequence alignment    



References

[1] Ester Serrano et al. (2021) Recombination proteins differently control the acquisition of homeologous DNA during Bacillus subtilis natural chromosomal transformation. Environmental Microbiology 23(1):512-524. [PMID: 33264457]
[2] Ester Serrano et al. (2018) RecA Regulation by RecU and DprA During Bacillus subtilis Natural Plasmid Transformation. Frontiers in Microbiology 9:1514. [PMID: 30050509]
[3] Shimin Le et al. (2017) Bacillus subtilis RecA with DprA-SsbA antagonizes RecX function during natural transformation. Nucleic Acids Research 45(15):8873-8885. [PMID: 28911099]
[4] Tribhuwan Yadav et al. (2014) Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination. The Journal of Biological Chemistry 289(40):27640-52. [PMID: 25138221]
[5] Tribhuwan Yadav et al. (2013) Bacillus subtilis DprA recruits RecA onto single-stranded DNA and mediates annealing of complementary strands coated by SsbB and SsbA. The Journal of Biological Chemistry 288(31):22437-50. [PMID: 23779106]
[6] Isabelle Mortier-Barrière et al. (2007) A key presynaptic role in transformation for a widespread bacterial protein: DprA conveys incoming ssDNA to RecA. Cell 130(5):824-36. [PMID: 17803906]
[7] Serkalem Tadesse et al. (2007) DprA/Smf protein localizes at the DNA uptake machinery in competent Bacillus subtilis cells. BMC Microbiology 7:105. [PMID: 18045469]