Detailed information NTG0000262

Experimentally validated

Overview

• Name: endA
• Type: Machinery gene
• Locus tag: KZH43_RS08770
• Genome accession: NZ_CP079923
• Coordinates: 1745343..1746167 (-)
• Length: 274 a.a.
• NCBI ID: WP_001036779.1
• Uniprot ID: P0A3S3
• Organism: Streptococcus pneumoniae Rx1
• Function: cleavage of dsDNA into ssDNA DNA processing

Function

EndA is a membrane-associated DNase essential for degrading one strand of internalized double-stranded DNA (dsDNA) during natural transformation. It degrades the nontransforming DNA strand, whereas the complementary transforming strand is transported into the cytoplasm in the 3' to 5' direction.

Genomic Context

Location: 1740343..1751167

Locus tag	Gene name	Coordinates (strand)	Size (bp)	Protein ID	Product	Description
KZH43_RS08765 (KZH43_08760)	-	1743783..1745114 (-)	1332	WP_000390046.1	hemolysin family protein	-
KZH43_RS08770 (KZH43_08765)	endA	1745343..1746167 (-)	825	WP_001036779.1	DNA-entry nuclease EndA	Machinery gene
KZH43_RS08775 (KZH43_08770)	-	1746206..1746394 (-)	189	WP_001036519.1	DNA-directed RNA polymerase subunit beta	-
KZH43_RS08780 (KZH43_08775)	murA	1746387..1747670 (-)	1284	WP_000358027.1	UDP-N-acetylglucosamine 1-carboxyvinyltransferase	-
KZH43_RS08785 (KZH43_08780)	-	1747694..1747924 (-)	231	WP_000250384.1	DUF1146 family protein	-
KZH43_RS08790 (KZH43_08785)	sepM	1747982..1749019 (-)	1038	WP_000727277.1	SepM family pheromone-processing serine protease	Regulator
KZH43_RS08795 (KZH43_08790)	coaD	1749003..1749491 (-)	489	WP_001280727.1	pantetheine-phosphate adenylyltransferase	-
KZH43_RS08800 (KZH43_08795)	rsmD	1749481..1750020 (-)	540	WP_000706962.1	16S rRNA (guanine(966)-N(2))-methyltransferase RsmD	-
KZH43_RS08805 (KZH43_08800)	asnA	1750085..1751077 (-)	993	WP_000747995.1	aspartate--ammonia ligase	-

Sequence

Protein

• Length: 274 a.a.
• Molecular weight: 29890.57 Da
• Isoelectric Point: 10.1197

>NTDB_id=262 KZH43_RS08770 WP_001036779.1 1745343..1746167(-) (endA) [Streptococcus pneumoniae Rx1]
MNKKTRQTLIGLLVLLLLSTGSYYIKQMPSAPNSPKTNLSQKKQASEAPSQALAESVLTDAVKSQIKGSLEWNGSGAFIV
NGNKTNLDAKVSSKPYADNKTKTVGKETVPTVANALLSKATRQYKNRKETGNGSTSWTPPGWHQVKNLKGSYTHAVDRGH
LLGYALIGGLDGFDASTSNPKNIAVQTAWANQAQAEYSTGQNYYESKVRKALDQNKRVRYRVTLYYASNEDLVPSASQIE
AKSSDGELEFNVLVPNVQKGLQLDYRTGEVTVTQ

Nucleotide

• Length: 825 bp

>NTDB_id=262 KZH43_RS08770 WP_001036779.1 1745343..1746167(-) (endA) [Streptococcus pneumoniae Rx1]
ATGAACAAAAAAACAAGACAGACACTAATCGGACTGCTAGTGTTATTGCTTTTGTCTACAGGGAGCTATTATATCAAGCA
GATGCCGTCGGCACCTAATAGTCCCAAAACCAATCTTAGTCAGAAAAAACAAGCGTCTGAAGCTCCTAGTCAAGCATTGG
CAGAGAGTGTCTTAACAGACGCAGTCAAGAGTCAAATAAAGGGGAGTCTGGAGTGGAATGGCTCAGGTGCTTTTATCGTC
AATGGTAATAAAACAAATCTAGATGCCAAGGTTTCAAGTAAGCCCTACGCTGACAATAAAACAAAGACAGTGGGCAAGGA
AACTGTTCCAACCGTAGCTAATGCCCTCTTGTCTAAGGCCACTCGTCAGTACAAGAATCGTAAAGAAACTGGGAATGGTT
CAACTTCTTGGACTCCTCCAGGTTGGCATCAGGTCAAGAATCTAAAGGGCTCTTATACCCATGCAGTCGATAGAGGTCAT
TTGTTAGGCTATGCCTTAATCGGTGGTTTGGATGGTTTTGATGCCTCAACAAGCAATCCTAAAAACATTGCTGTTCAGAC
AGCCTGGGCAAATCAGGCACAAGCCGAGTATTCGACTGGTCAAAACTACTATGAAAGCAAGGTGCGTAAAGCCTTGGACC
AAAACAAGCGTGTCCGTTACCGTGTAACCCTTTACTACGCTTCAAACGAGGATTTAGTTCCCTCAGCTTCACAGATTGAA
GCCAAGTCTTCGGATGGAGAATTGGAATTCAATGTTCTAGTTCCCAATGTTCAAAAGGGACTTCAACTGGATTACCGAAC
TGGAGAAGTAACTGTAACTCAGTAA

Domains

Predicted by InterproScan.

• DNA/RNA non-specific endonuclease (Endonuclease_NS) (75-247)

3D structure

• PDB: 3OWV

Similar proteins

Only experimentally validated proteins are listed.

Protein	Organism	Identities (%)	Coverage (%)	Ha-value
endA	Streptococcus pneumoniae R6	100	100	1
endA	Streptococcus pneumoniae D39	100	100	1
endA	Streptococcus pneumoniae TIGR4	100	100	1

References

• [1]: Malik Amonov et al. (2020) Disruption of the cpsE and endA Genes Attenuates Streptococcus pneumoniae Virulence: Towards the Development of a Live Attenuated Vaccine Candidate. Vaccines 8(2):187. [PMID: 32326482]
• [2]: Eliza J R Peterson et al. (2013) Inhibitors of Streptococcus pneumoniae surface endonuclease EndA discovered by high-throughput screening using a PicoGreen fluorescence assay. Journal of Biomolecular Screening 18(3):247-57. [PMID: 23015019]
• [3]: Luchang Zhu et al. (2013) Competence-independent activity of pneumococcal EndA [corrected] mediates degradation of extracellular dna and nets and is important for virulence. PloS One 8(7):e70363. [PMID: 23936195]
• [4]: Matthieu J Bergé et al. (2013) Midcell recruitment of the DNA uptake and virulence nuclease, EndA, for pneumococcal transformation. PLoS Pathogens 9(9):e1003596. [PMID: 24039578]
• [5]: Marika Midon et al. (2012) Chemical rescue of active site mutants of S. pneumoniae surface endonuclease EndA and other nucleases of the HNH family by imidazole. Chembiochem : A European Journal of Chemical Biology 13(5):713-21. [PMID: 22344704]
• [6]: Marika Midon et al. (2011) Mutational and biochemical analysis of the DNA-entry nuclease EndA from Streptococcus pneumoniae. Nucleic Acids Research 39(2):623-34. [PMID: 20846957]
• [7]: Andrea F Moon et al. (2011) Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae. Nucleic Acids Research 39(7):2943-53. [PMID: 21113026]
• [8]: Katharina Beiter et al. (2006) An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Current Biology : CB 16(4):401-7. [PMID: 16488875]
• [9]: Mathieu Bergé et al. (2002) Uptake of transforming DNA in Gram-positive bacteria: a view from Streptococcus pneumoniae. Molecular Microbiology 45(2):411-21. [PMID: 12123453]
• [10]: V Méjean et al. (1993) DNA processing during entry in transformation of Streptococcus pneumoniae. The Journal of Biological Chemistry 268(8):5594-9. [PMID: 8449922]
• [11]: A Puyet et al. (1990) Genetic and structural characterization of endA. A membrane-bound nuclease required for transformation of Streptococcus pneumoniae. Journal of Molecular Biology 213(4):727-38. [PMID: 2359120]