Detailed information NTG0000157

Experimentally validated

Overview

• Name: dprA/cilB/dalA
• Type: Machinery gene
• Locus tag: SP_RS06205
• Genome accession: NC_003028
• Coordinates: 1199284..1200132 (-)
• Length: 282 a.a.
• NCBI ID: WP_000705306.1
• Uniprot ID: A0A098Z7D2
• Organism: Streptococcus pneumoniae TIGR4
• Function: ssDNA binding; loading RecA onto ssDNA; competence shut-off DNA processing Competence regulation

Function

In S. pneumoniae, it was found that DprA plays a dual role. First, DprA (DNA Processing Protein A) is essential for protecting internalized single-stranded DNA (ssDNA) and facilitating its loading onto RecA recombinase during natural transformation. Second, DprA also mediates competence shut-off by dissociating ComE∼P dimers from the promoters of the early competence genes.

Genomic Context

Location: 1194284..1205132

Locus tag	Gene name	Coordinates (strand)	Size (bp)	Protein ID	Product	Description
SP_RS06195 (SP_1263)	topA	1195085..1197184 (-)	2100	WP_000179649.1	type I DNA topoisomerase	-
SP_RS06200 (SP_1264)	-	1197351..1198394 (-)	1044	WP_001812957.1	TIGR00341 family protein	-
SP_RS13660	-	1198978..1199100 (+)	123	WP_001814242.1	hypothetical protein	-
SP_RS06205 (SP_1266)	dprA/cilB/dalA	1199284..1200132 (-)	849	WP_000705306.1	DNA-processing protein DprA	Machinery gene
SP_RS06210 (SP_1267)	-	1200228..1200917 (-)	690	WP_000643971.1	sugar phosphate nucleotidyltransferase	-
SP_RS06215 (SP_1268)	-	1200929..1201807 (-)	879	WP_000837617.1	DMT family transporter	-
SP_RS06220 (SP_1269)	licA	1201797..1202666 (-)	870	WP_000411215.1	choline kinase LicA	-
SP_RS06225 (SP_1270)	-	1202683..1203705 (-)	1023	WP_000609885.1	ribitol-5-phosphate dehydrogenase	-
SP_RS06230 (SP_1271)	-	1203710..1204417 (-)	708	WP_000638508.1	IspD/TarI family cytidylyltransferase	-

Sequence

Protein

• Length: 282 a.a.
• Molecular weight: 31062.72 Da
• Isoelectric Point: 5.4047

>NTDB_id=157 SP_RS06205 WP_000705306.1 1199284..1200132(-) (dprA/cilB/dalA) [Streptococcus pneumoniae TIGR4]
MKITNYEIYKLKKSGLTNQQILKVLEYGENVDQELLLGDIADISGCRNPAVFMERYFQIDDAHLSKEFQKFPSFSILDDC
YPWDLSEIYDAPVLLFYKGNLDLLKFPKVAVVGSRACSKQGAKSVEKVIQGLENELVIVSGLAKGIDTAAHMAALQNGGK
TIAVIGTGLDVFYPKANKRLQDYIGNDHLVLSEYGPGEQPLKFHFPARNRIIAGLCRGVIVAEAKMRSGSLITCERAMEE
GRDVFAIPGSILDGLSDGCHHLIQEGAKLVTSGQDVLAEFEF

Nucleotide

• Length: 849 bp

>NTDB_id=157 SP_RS06205 WP_000705306.1 1199284..1200132(-) (dprA/cilB/dalA) [Streptococcus pneumoniae TIGR4]
ATGAAAATCACAAACTATGAAATCTATAAGTTAAAAAAATCAGGTTTGACCAATCAACAGATTTTGAAAGTGCTAGAATA
CGGTGAAAATGTTGATCAGGAGCTTTTGTTGGGTGATATTGCAGATATCTCAGGTTGCCGTAATCCAGCCGTTTTTATGG
AACGTTATTTTCAGATAGACGATGCGCATTTGTCGAAAGAGTTTCAAAAATTTCCATCTTTCTCTATTTTAGATGACTGT
TATCCTTGGGATTTGAGTGAAATATATGATGCGCCTGTACTTTTATTTTACAAGGGAAATCTTGACCTCCTGAAATTCCC
GAAGGTAGCGGTCGTGGGCAGTCGTGCTTGTAGCAAACAGGGAGCTAAGTCAGTTGAAAAAGTCATTCAAGGCTTGGAAA
ATGAACTGGTTATTGTCAGTGGTCTGGCCAAGGGCATTGACACAGCAGCTCATATGGCAGCTCTTCAGAATGGCGGAAAA
ACCATTGCAGTGATTGGAACAGGACTGGATGTGTTTTATCCTAAAGCCAATAAACGCTTGCAAGACTACATCGGCAATGA
CCATCTGGTTCTAAGTGAATATGGACCTGGTGAACAACCTCTGAAATTTCATTTTCCTGCCCGTAATCGCATCATTGCTG
GACTTTGTCGTGGTGTGATTGTAGCAGAGGCTAAGATGCGTTCAGGTAGTCTCATTACGTGTGAGCGAGCAATGGAAGAA
GGACGCGATGTCTTTGCTATTCCTGGTAGCATTTTAGATGGACTATCAGACGGTTGCCATCATTTGATTCAAGAAGGAGC
AAAATTGGTCACCAGTGGGCAAGATGTTCTTGCGGAATTTGAATTTTAA

Domains

Predicted by InterproScan.

• DNA recombination-mediator protein A (DNA_processg_A) (75-271)

• DNA processing protein A sterile alpha motif domain (SAM_DprA) (3-64)

3D structure

• AlphaFold DB: A0A098Z7D2

Similar proteins

Only experimentally validated proteins are listed.

Protein	Organism	Identities (%)	Coverage (%)	Ha-value
dprA/cilB/dalA	Streptococcus pneumoniae R6	100	100	1
dprA/cilB/dalA	Streptococcus pneumoniae D39	100	100	1
dprA/cilB/dalA	Streptococcus pneumoniae Rx1	100	100	1
dprA/cilB/dalA	Streptococcus mitis NCTC 12261	98.582	100	0.986
dprA/cilB/dalA	Streptococcus mitis SK321	97.872	100	0.979
dprA	Streptococcus mutans UA159	63.214	100	0.632
dprA	Lactococcus lactis subsp. cremoris KW2	55.714	99.291	0.553
dprA	Staphylococcus aureus N315	37.809	100	0.379
dprA	Haemophilus influenzae Rd KW20	38.202	94.681	0.362

References

• [1]: Jingjun Lin et al. (2020) Streptococcus pneumoniae Elaborates Persistent and Prolonged Competent State during Pneumonia-Derived Sepsis. Infection And Immunity 88(4):e00919-19. [PMID: 31988172]
• [2]: Calum Hg Johnston et al. (2020) The alternative sigma factor σ^X mediates competence shut-off at the cell pole in Streptococcus pneumoniae. ELife 9:e62907. [PMID: 33135635]
• [3]: Jingjun Lin et al. (2019) DprA-Dependent Exit from the Competent State Regulates Multifaceted Streptococcus pneumoniae Virulence. Infection And Immunity 87(11):e00349-19. [PMID: 31451619]
• [4]: Calum Johnston et al. (2018) Fine-tuning cellular levels of DprA ensures transformant fitness in the human pathogen Streptococcus pneumoniae. Molecular Microbiology 109(5):663-675. [PMID: 29995987]
• [5]: Mathias Weyder et al. (2018) Dynamic Modeling of Streptococcus pneumoniae Competence Provides Regulatory Mechanistic Insights Into Its Tight Temporal Regulation. Frontiers in Microbiology 9:1637. [PMID: 30087661]
• [6]: Yi Yu et al. (2017) The virulence of Streptococcus pneumoniae partially depends on dprA. Brazilian Journal of Microbiology : [publication of The Brazilian Society For Microbiology] 48(2):225-231. [PMID: 28011228]
• [7]: Amy Diallo et al. (2017) Bacterial transformation: ComFA is a DNA-dependent ATPase that forms complexes with ComFC and DprA. Molecular Microbiology 105(5):741-754. [PMID: 28618091]
• [8]: Johnny Lisboa et al. (2014) Molecular determinants of the DprA-RecA interaction for nucleation on ssDNA. Nucleic Acids Research 42(11):7395-408. [PMID: 24782530]
• [9]: Nicolas Mirouze et al. (2013) Direct involvement of DprA, the transformation-dedicated RecA loader, in the shut-off of pneumococcal competence. Proceedings of The National Academy of Sciences of The United States of America 110(11):E1035-44. [PMID: 23440217]
• [10]: Liming Weng et al. (2013) Exit from competence for genetic transformation in Streptococcus pneumoniae is regulated at multiple levels. PloS One 8(5):e64197. [PMID: 23717566]
• [11]: Sophie Quevillon-Cheruel et al. (2012) Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation. Proceedings of The National Academy of Sciences of The United States of America 109(37):E2466-75. [PMID: 22904190]
• [12]: 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]
• [13]: Scott N Peterson et al. (2004) Identification of competence pheromone responsive genes in Streptococcus pneumoniae by use of DNA microarrays. Molecular Microbiology 51(4):1051-70. [PMID: 14763980]
• [14]: Mathieu Bergé et al. (2003) Transformation of Streptococcus pneumoniae relies on DprA- and RecA-dependent protection of incoming DNA single strands. Molecular Microbiology 50(2):527-36. [PMID: 14617176]