Detailed information
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 |
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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
MEKEKKGAKHELDLSSILQFVAPGTPLRAGMENVLRANTGGLIVVGYNDKVKEVVDGGFHINTAFSPAHLYELAKMDGAI
ILSDSGQKILYANTQLMPDATISSSETGMRHRTAERVAKQTGCLVIAISERRNVITLYQENMKYTLKDIGFILTKANQAI
QTLEKYKTILDKTINALNALEFEELVTFSDVLSVMHRYEMVLRIKNEINMYIKELGTEGHLIKLQVIELITDMEEEAALF
IKDYVKEKIKDPFVLLKELQDMSSYDLLDDSIVYKLLGYPASTNLDDYVLPRGYRLLNKIPRLPMPIVENVVEAFGVLPR
IIEASAEELDEVEGIGEVRAQKIKKGLKRLQEKHYLDRQL
Nucleotide
Download Length: 1083 bp
ATGGAAAAAGAGAAAAAAGGGGCGAAACACGAGTTAGACCTGTCATCTATATTGCAGTTTGTTGCTCCGGGTACACCGCT
CAGAGCGGGGATGGAAAACGTCTTGAGAGCAAATACAGGCGGTCTGATTGTTGTTGGATATAATGATAAAGTAAAAGAAG
TGGTGGACGGCGGCTTTCACATAAACACGGCTTTTTCTCCGGCGCATTTATATGAGCTGGCTAAAATGGATGGAGCGATC
ATTTTAAGTGATTCTGGTCAAAAGATCCTATACGCGAATACTCAGCTGATGCCGGATGCCACAATTTCTTCATCAGAAAC
AGGAATGCGGCACAGAACTGCCGAAAGAGTAGCTAAGCAAACTGGCTGTCTTGTAATCGCCATTTCTGAAAGAAGAAATG
TCATAACGTTATATCAGGAAAACATGAAGTATACACTAAAAGACATAGGATTTATTTTAACCAAGGCGAACCAAGCCATT
CAAACACTTGAAAAATATAAGACAATCCTCGATAAAACGATTAATGCACTGAACGCGTTAGAGTTTGAGGAACTTGTTAC
CTTCAGTGATGTCTTGTCTGTCATGCATCGTTATGAAATGGTACTGAGAATCAAAAACGAAATTAATATGTATATCAAAG
AGCTGGGGACAGAAGGGCATCTGATCAAACTGCAAGTCATTGAATTGATTACGGATATGGAAGAAGAGGCCGCTTTATTT
ATTAAGGACTATGTAAAAGAAAAGATTAAAGATCCGTTTGTTCTCTTGAAGGAGCTGCAGGATATGTCCAGTTATGATCT
GCTGGATGATTCCATTGTGTATAAGCTTCTCGGTTACCCTGCTTCTACTAATCTTGATGATTATGTATTGCCGAGAGGAT
ACAGGCTGTTAAATAAGATACCGCGTCTTCCGATGCCGATTGTTGAAAATGTTGTAGAAGCATTTGGAGTCCTGCCAAGG
ATTATTGAGGCGAGTGCAGAAGAATTAGATGAAGTAGAGGGAATCGGTGAAGTACGAGCCCAAAAAATCAAAAAAGGATT
AAAACGCCTGCAAGAGAAGCATTATTTAGACAGACAACTGTGA
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] |