Detailed information    

experimental Experimentally validated

Overview


Name   disA   Type   Machinery gene
Locus tag   BSU_00880 Genome accession   NC_000964
Coordinates   107476..108558 (+) Length   360 a.a.
NCBI ID   NP_387969.1    Uniprot ID   P37573
Organism   Bacillus subtilis subsp. subtilis str. 168     
Function   homologous recombination   
Homologous recombination

Function


DisA is necessary to coordinate responses to replicative stress; it could help to circumvent damaged template bases that otherwise impede fork progression. RecG-mediated fork remodeling is a genuine in vivo activity, and that DisA, as a molecular switch, limits RecG-mediated fork reversal and fork restoration. DisA and RecG might provide more time to process perturbed forks, avoiding genome breakage. DisA signals DNA structures that interfere with chromosome segregation via c-di-AMP. RuvAB or RecU pre-bound to HJ DNA strongly inhibits DisA-mediated synthesis of c-di-AMP, and indirectly blocks cell proliferation. DisA limits the ssDNA-dependent ATPase activity of RadA/Sms C13A, and inhibits the helicase activity of RadA/Sms by a protein-protein interaction. RadA/Sms inhibits DisA-mediated c-di-AMP synthesis and indirectly inhibits cell proliferation, but RecA counters this negative effect.


Genomic Context


Location: 102476..113558
Locus tag Gene name Coordinates (strand) Size (bp) Protein ID Product Description
  BSU_00850 (BSU00850) mcsB 102484..103575 (+) 1092 NP_387966.1 protein arginine kinase -
  BSU_00860 (BSU00860) clpC 103572..106004 (+) 2433 NP_387967.1 class III stress response-related ATPase, AAA+ superfamily Regulator
  BSU_00870 (BSU00870) radA/sms 106096..107472 (+) 1377 NP_387968.1 DNA repair protein; 6-O-methylguanine-DNA methyltransferase Machinery gene
  BSU_00880 (BSU00880) disA 107476..108558 (+) 1083 NP_387969.1 diadenylate cyclase; DNA integrity scanning protein; cell cycle checkpoint DNA scanning protein Machinery gene
  BSU_00890 (BSU00890) yacL 108674..109774 (+) 1101 NP_387970.1 putative membrane protein possibly involved in RNA binding -
  BSU_00900 (BSU00900) ispD 109789..110487 (+) 699 NP_387971.1 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, nonmevalonate isoprenoid pathway -
  BSU_00910 (BSU00910) ispF 110480..110956 (+) 477 NP_387972.1 2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase -
  BSU_00920 (BSU00920) gltX 111047..112498 (+) 1452 NP_387973.1 glutamyl-tRNA synthetase -
  BSU_00930 (BSU00930) cysE 112800..113453 (+) 654 NP_387974.1 serine O-acetyltransferase -

Sequence


Protein


Download         Length: 360 a.a.        Molecular weight: 40734.29 Da        Isoelectric Point: 5.7343

>NTDB_id=634 BSU_00880 NP_387969.1 107476..108558(+) (disA) [Bacillus subtilis subsp. subtilis str. 168]
MEKEKKGAKHELDLSSILQFVAPGTPLRAGMENVLRANTGGLIVVGYNDKVKEVVDGGFHINTAFSPAHLYELAKMDGAI
ILSDSGQKILYANTQLMPDATISSSETGMRHRTAERVAKQTGCLVIAISERRNVITLYQENMKYTLKDIGFILTKANQAI
QTLEKYKTILDKTINALNALEFEELVTFSDVLSVMHRYEMVLRIKNEINMYIKELGTEGHLIKLQVIELITDMEEEAALF
IKDYVKEKIKDPFVLLKELQDMSSYDLLDDSIVYKLLGYPASTNLDDYVLPRGYRLLNKIPRLPMPIVENVVEAFGVLPR
IIEASAEELDEVEGIGEVRAQKIKKGLKRLQEKHYLDRQL

Nucleotide


Download         Length: 1083 bp        

>NTDB_id=634 BSU_00880 NP_387969.1 107476..108558(+) (disA) [Bacillus subtilis subsp. subtilis str. 168]
ATGGAAAAAGAGAAAAAAGGGGCGAAACACGAGTTAGACCTGTCATCTATATTGCAGTTTGTTGCTCCGGGTACACCGCT
CAGAGCGGGGATGGAAAACGTCTTGAGAGCAAATACAGGCGGTCTGATTGTTGTTGGATATAATGATAAAGTAAAAGAAG
TGGTGGACGGCGGCTTTCACATAAACACGGCTTTTTCTCCGGCGCATTTATATGAGCTGGCTAAAATGGATGGAGCGATC
ATTTTAAGTGATTCTGGTCAAAAGATCCTATACGCGAATACTCAGCTGATGCCGGATGCCACAATTTCTTCATCAGAAAC
AGGAATGCGGCACAGAACTGCCGAAAGAGTAGCTAAGCAAACTGGCTGTCTTGTAATCGCCATTTCTGAAAGAAGAAATG
TCATAACGTTATATCAGGAAAACATGAAGTATACACTAAAAGACATAGGATTTATTTTAACCAAGGCGAACCAAGCCATT
CAAACACTTGAAAAATATAAGACAATCCTCGATAAAACGATTAATGCACTGAACGCGTTAGAGTTTGAGGAACTTGTTAC
CTTCAGTGATGTCTTGTCTGTCATGCATCGTTATGAAATGGTACTGAGAATCAAAAACGAAATTAATATGTATATCAAAG
AGCTGGGGACAGAAGGGCATCTGATCAAACTGCAAGTCATTGAATTGATTACGGATATGGAAGAAGAGGCCGCTTTATTT
ATTAAGGACTATGTAAAAGAAAAGATTAAAGATCCGTTTGTTCTCTTGAAGGAGCTGCAGGATATGTCCAGTTATGATCT
GCTGGATGATTCCATTGTGTATAAGCTTCTCGGTTACCCTGCTTCTACTAATCTTGATGATTATGTATTGCCGAGAGGAT
ACAGGCTGTTAAATAAGATACCGCGTCTTCCGATGCCGATTGTTGAAAATGTTGTAGAAGCATTTGGAGTCCTGCCAAGG
ATTATTGAGGCGAGTGCAGAAGAATTAGATGAAGTAGAGGGAATCGGTGAAGTACGAGCCCAAAAAATCAAAAAAGGATT
AAAACGCCTGCAAGAGAAGCATTATTTAGACAGACAACTGTGA


Secondary structure


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



3D structure


Source ID Structure
  AlphaFold DB P37573

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

References


[1] Alejandra Rangel-Mendoza et al. (2025) Germination and Outgrowth of Bacillus subtilis Spores Deficient in BER and DisA Unveil Alternative Genetic Checkpoints. Microorganisms 13(4):939. [PMID: 40284773]
[2] Rubén Torres et al. (2021) DisA Limits RecG Activities at Stalled or Reversed Replication Forks. Cells 10(6):1357. [PMID: 34073022]
[3] Carolina Gándara et al. (2021) DisA Restrains the Processing and Cleavage of Reversed Replication Forks by the RuvAB-RecU Resolvasome. International Journal of Molecular Sciences 22(21):11323. [PMID: 34768753]
[4] Rubén Torres et al. (2021) Bacillus subtilis RecA, DisA, and RadA/Sms Interplay Prevents Replication Stress by Regulating Fork Remodeling. Frontiers in Microbiology 12:766897. [PMID: 34880841]
[5] Luz I Valenzuela-García et al. (2018) Transcriptional coupling (Mfd) and DNA damage scanning (DisA) coordinate excision repair events for efficient Bacillus subtilis spore outgrowth. MicrobiologyOpen 7(5):e00593. [PMID: 29536659]
[6] Carolina Gándara et al. (2017) Activity and in vivo dynamics of Bacillus subtilis DisA are affected by RadA/Sms and by Holliday junction-processing proteins. DNA Repair 55:17-30. [PMID: 28511132]
[7] Marina Raguse et al. (2017) Bacillus subtilis DisA helps to circumvent replicative stress during spore revival. DNA Repair 59:57-68. [PMID: 28961460]
[8] Clement Opoku-Temeng et al. (2016) Inhibition of cyclic diadenylate cyclase, DisA, by polyphenols. Scientific Reports 6:25445. [PMID: 27150552]
[9] Carolina Gándara et al. (2015) DisA and c-di-AMP act at the intersection between DNA-damage response and stress homeostasis in exponentially growing Bacillus subtilis cells. DNA Repair 27:1-8. [PMID: 25616256]
[10] Silvia S Campos et al. (2014) Interaction of apurinic/apyrimidinic endonucleases Nfo and ExoA with the DNA integrity scanning protein DisA in the processing of oxidative DNA damage during Bacillus subtilis spore outgrowth. Journal of Bacteriology 196(3):568-78. [PMID: 24244006]
[11] Gregor Witte et al. (2008) Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Molecular Cell 30(2):167-78. [PMID: 18439896]