Detailed information of TA system    

experimentalExperimentally validated    

Overview


TA module


Type II Classification (family/domain) rnlAB/-
Location 2765918..2767355 Replicon chromosome
Accession NC_000913
Organism Escherichia coli str. K-12 substr. MG1655

Toxin (Protein)


Gene name rnlA Uniprot ID P52129
Locus tag b2630 Protein ID NP_417119.1
Coordinates 2765918..2766991 (+) Length 358 a.a.

Antitoxin (Protein)


Gene name rnlB Uniprot ID P52130
Locus tag b2631 Protein ID NP_417120.2
Coordinates 2766984..2767355 (+) Length 124 a.a.

Genomic Context


Locus tag Coordinates Strand Size (bp) Protein ID Product Description
b2627 2761351..2763540 - 2190 NP_417116.1 putative helicase YfjK -
b2628 2763537..2765153 - 1617 NP_417117.1 anti-bacteriophage protein -
b2629 2765513..2765776 - 264 NP_417118.1 protein YfjM -
b2630 2765918..2766991 + 1074 NP_417119.1 RNase LS, toxin of the RnlAB toxin-antitoxin system Toxin
b2631 2766984..2767355 + 372 NP_417120.2 antitoxin RnlB Antitoxin
b2632 2767710..2768573 + 864 YP_026173.1 putative GTP-binding protein YfjP -
b2633 2768665..2769486 + 822 NP_417122.1 DUF932 domain-containing protein YfjQ -
b2634 2769703..2770404 + 702 NP_417123.1 putative DNA-binding transcriptional regulator YfjR -
b2635 2770445..2770681 + 237 YP_026174.2 uncharacterized protein YpjK -
b2636 2770681..2771124 + 444 NP_417124.4 inner membrane lipoprotein YfjS -
b2637 2771148..2771615 + 468 NP_417125.1 uncharacterized protein YfjT -
b2638 2771840..2772154 - 315 YP_009518807.1 putative arsenate reductase-like protein YfjU -

Associated MGEs


MGE
detail
Similar
MGEs
Relative
position
MGE Type Cargo ARG Virulence gene Coordinates Length (bp)


Relative position:
(1) inside: TA loci is completely located inside the MGE;
(2) overlap: TA loci is partially overlapped with the MGE;
(3) flank: The TA loci is located in the 5 kb flanking regions of MGE.



Sequences


Toxin        


Download         Length: 358 a.a.        Molecular weight: 40061.13 Da        Isoelectric Point: 6.8293

>T6077 NP_417119.1 NC_000913:2765918-2766991 [Escherichia coli str. K-12 substr. MG1655]
MTIRSYKNLNLVRANIETESRQFIENKNYSIQSIGPMPGSRAGLRVVFTRPGVNLATVDIFYNGDGSTTIQYLTGANRSL
GQELADHLFETINPAEFEQVNMVLQGFVETSVLPVLELSADESHIEFREHSRNAHTVVWKIISTSYQDELTVSLHITTGK
LQIQGRPLSCYRVFTFNLAALLDLQGLEKVLIRQEDGKANIVQQEVARTYLQTVMADAYPHLHVTAEKLLVSGLCVKLAA
PDLPDYCMLLYPELRTIEGVLKSKMSGLGMPVQQPAGFGTYFDKPAAHYILKPQFAATLRPEQINIISTAYTFFNVERHS
LFHMETVVDASRMISDMARLMGKATRAWGIIKDLYIV

Download         Length: 1074 bp

>T6077 NC_000913:2765918-2766991 [Escherichia coli str. K-12 substr. MG1655]
ATGACAATCAGGAGTTACAAAAACTTAAATCTGGTCAGGGCAAATATCGAGACTGAATCCAGACAATTCATTGAAAATAA
AAACTATTCAATCCAATCAATTGGTCCTATGCCAGGGTCAAGGGCTGGGCTTCGGGTCGTATTTACCAGACCAGGGGTTA
ACTTGGCAACTGTGGACATTTTTTATAACGGGGACGGTTCGACTACAATTCAATATCTCACTGGAGCCAATCGTTCTCTG
GGCCAAGAGTTAGCGGATCATCTTTTTGAAACCATCAATCCTGCTGAATTTGAGCAGGTAAATATGGTACTGCAAGGATT
TGTAGAGACAAGCGTTCTACCTGTACTTGAGCTATCAGCAGATGAATCGCATATAGAGTTCAGAGAACACTCTCGTAACG
CTCATACCGTAGTGTGGAAAATTATTTCCACCAGCTATCAGGACGAATTGACTGTGAGCCTGCATATCACAACAGGTAAG
CTCCAGATTCAGGGCCGACCGCTGTCATGTTACAGAGTTTTCACGTTTAACTTGGCAGCCCTGCTTGATTTACAGGGTTT
GGAGAAAGTGCTAATCCGCCAGGAGGATGGTAAAGCTAATATTGTTCAACAGGAGGTTGCCCGCACTTACTTGCAGACTG
TAATGGCCGATGCTTACCCGCATCTCCACGTGACTGCCGAAAAATTGCTCGTTTCAGGGCTATGTGTTAAACTCGCCGCC
CCTGATTTGCCTGACTACTGTATGTTACTTTATCCTGAACTACGCACCATTGAAGGTGTCTTAAAAAGTAAGATGAGTGG
GTTAGGCATGCCAGTACAGCAGCCGGCAGGTTTTGGAACTTACTTTGATAAACCTGCTGCTCATTACATTCTGAAACCGC
AATTTGCAGCTACTCTTAGACCGGAACAGATTAACATCATCAGCACAGCCTATACTTTTTTTAATGTGGAACGTCATTCT
CTGTTCCACATGGAAACTGTGGTCGATGCCAGCCGTATGATTTCTGATATGGCCCGGTTGATGGGTAAAGCCACTAGAGC
GTGGGGAATAATCAAGGACTTATATATTGTTTGA

Antitoxin


Download         Length: 124 a.a.        Molecular weight: 13664.69 Da        Isoelectric Point: 4.2391

>AT6077 NP_417120.2 NC_000913:2766984-2767355 [Escherichia coli str. K-12 substr. MG1655]
MFEITGINVSGALKAVVMATGFENPLSSVNEIETKLSALLGSETTGEILFDLLCANGPEWNRFVTLEMKYGRIMLDTAKI
IDEQDVPTHILSKLTFTLRNHPEYLEASVLSPDDVRQVLSMDF

Download         Length: 372 bp

>AT6077 NC_000913:2766984-2767355 [Escherichia coli str. K-12 substr. MG1655]
TTGTTTGAAATCACCGGAATTAACGTCTCAGGGGCTCTAAAAGCTGTCGTTATGGCGACCGGCTTCGAGAACCCTTTGTC
CTCAGTTAATGAAATTGAGACGAAACTTTCTGCCCTACTGGGTAGTGAGACCACTGGTGAAATCCTTTTTGACCTCTTGT
GCGCTAACGGTCCAGAGTGGAACCGCTTCGTTACGCTGGAAATGAAATATGGCCGGATCATGCTGGATACGGCCAAAATT
ATTGATGAGCAGGACGTTCCGACACATATCCTGAGCAAACTGACTTTTACTTTACGTAATCATCCTGAGTACCTAGAAGC
CTCTGTTTTGTCTCCCGATGATGTACGCCAAGTCCTGTCAATGGATTTTTGA

Similar Proteins


Only experimentally validated proteins are listed.

Protein Organism Identities (%) Coverage (%) Ha-value
T6075 Escherichia coli DH1

100

100

1

T6076 Escherichia coli BW2952

100

100

1

T10023 Escherichia coli BW25113

100

100

1

T10022 Escherichia coli str. K-12 substr. W3110 strain K-12 substr. ZK126

100

100

1


Multiple sequence alignment    


Protein Organism Identities (%) Coverage (%) Ha-value
AT6075 Escherichia coli DH1

100

100

1

AT6076 Escherichia coli BW2952

100

100

1

AT10023 Escherichia coli BW25113

100

100

1

AT10022 Escherichia coli str. K-12 substr. W3110 strain K-12 substr. ZK126

100

100

1


Multiple sequence alignment    




Structures


Toxin

Source ID Structure
PDB 6Y2R
PDB 7AEX
PDB 6Y2Q
PDB 4I8O
PDB 6Y2P
PDB 6Y2S


Antitoxin

Source ID Structure
PDB 6Y2P
AlphaFold DB P52130

References


(1) Gabriela Garcia-Rodriguez et al. (2021) Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA. Nucleic Acids Research 49(12):7164-7178. [PubMed:34139012] 3D_structure

(2) Mitsunori Koga et al. (2011) Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system. Genetics 187(1):123-30. [PubMed:20980243] experimental

(3) Francesca L Short et al. (2012) A promiscuous antitoxin of bacteriophage T4 ensures successful viral replication. Molecular Microbiology 83(4):665-8. [PubMed:22283468] experimental

(4) Yuichi Otsuka et al. (2012) Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli LsoA and RnlA toxins. Molecular Microbiology 83(4):669-81. [PubMed:22403819] experimental

(5) Nava Hosseini et al. (2019) Modulation of Toxin-Antitoxin System Rnl AB Type II in Phage-Resistant Gammaproteobacteria Surviving Photodynamic Treatment. Journal of Lasers in Medical Sciences 10(1):21-28. [PubMed:31360364]

(6) Yong Wei et al. (2016) Structural characterizations of phage antitoxin Dmd and its interactions with bacterial toxin RnlA. Biochemical And Biophysical Research Communications 472(4):592-7. [PubMed:26972252] 3D_structure

(7) Gabriela Garcia-Rodriguez et al. (2020) The Escherichia coli RnlA-RnlB toxin-antitoxin complex: production, characterization and crystallization. Acta Crystallographica. Section F, Structural Biology Communications 76(Pt 1):31-39. [PubMed:31929184] 3D_structure

(8) Miyuki Tsukuda et al. (2015) Counterselection method based on conditional silencing of antitoxin genes in Escherichia coli. Journal of Bioscience And Bioengineering 120(5):591-5. [PubMed:25912447] experimental

(9) Yong Wei et al. (2013) Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance. Molecular Microbiology 90(5):956-65. [PubMed:24112600] 3D_structure

(10) Kenta Naka et al. (2017) RnlB Antitoxin of the Escherichia coli RnlA-RnlB Toxin-Antitoxin Module Requires RNase HI for Inhibition of RnlA Toxin Activity. Toxins 9(1):29. [PubMed:28085056] in_silico

(11) Kenta Naka et al. (2014) RNase HI stimulates the activity of RnlA toxin in Escherichia coli. Molecular Microbiology 91(3):596-605. [PubMed:24308852] experimental


experimental experimental literature
in_silico in silico analysis literature
3D_structure protein structure literature