vapC4



Type
protein_coding
Name
vapC4
Locus Name

Rv0595c

Product

Possible toxin VapC4

Functional Category

Virulence, detoxification, adaptation

Location
694839..695231 (- strand)
Gene Length
392 bp
Nucleotides
GTGAACGTACGGCGCGCCCTCGCCGACACATCCGTTTTCATTGGCATCGAGGCGACACGATTCGACCCGGACCGGTTTGCGGGATACGAATGGGGCGTCTCGGTAGTCACACTCGGCGAGCTGCGGCTCGGGGTGTTGCAAGCCTCCGGCCCCGAGGCCGCCGCACGTCGGCTCTCCACCTACCAGCTTGCGCAACGGTTCGAACCACTAGGCATCGACGAGGCGGTCTCCGAAGCATGGGCATTACTGGTGTCCAAGCTGCGCGCCGCCAAACTGCGCGTGCCGATCAACGACAGCTGGATTGCGGCCACAGCCGTGGCGCACGGCATTGCGATCCTGACCCAAGACAACGACTACGCCGCCATGCCCGACGTCGAGGTCATAACGATCTG
Drug Resistance

Check for drug resistance association at TBDREAMDB

Mutations

Check for mutants available at TARGET


Function
Toxic component of a type II toxin-antitoxin (TA) system. Probably exerts its toxic effect by binding to mRNA, inhibiting translation. Binds to, recognizes and cleaves ssRNA at ACGC and AC(A/U)GC sequences, usually between the G and C; cleavage is not very efficient, nor is cleavage required to inhibit protein synthesis. Upon expression in situ, in M.smegmatis or E.coli inhibits cell growth and colony formation; in at least E.coli also causes increased levels of cellular RNA. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB4. {ECO:0000269|PubMed:19016878, ECO:0000269|PubMed:22354968, ECO:0000269|PubMed:25622615}.
Family

PINc/VapC protein family

GO
InterPro

UniProt
O07783
GenBank
Rv0595c
EnsemblBacteria
Rv0595c
Mycobrowser
Rv0595c


Summary
Name
Ribonuclease VapC4 (RNase VapC4) (EC 3.1.-.-) (Toxin VapC4) (VapC-mt4)
Family
PINc/VapC protein family
Protein Sequence
MNVRRALADTSVFIGIEATRFDPDRFAGYEWGVSVVTLGELRLGVLQASGPEAAARRLSTYQLAQRFEPLGIDEAVSEAWALLVSKLRAAKLRVPINDSWIAATAVAHGIAILTQDNDYAAMPDVEVITI
Mass
14,112 Da
Length
130 Aa

Rv0595c doesn't seem to be a targeted by any drug.


Rv0595c doesn't seem to be involved in any pathway.


Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding module.
J Bacteriol. 2015 Apr;197(7):1197-207. doi: 10.1128/JB.02508-14. Epub 2015 Jan 26.
Proteomic profiling of Mycobacterium tuberculosis identifies nutrient-starvation-responsive toxin-antitoxin systems.
Mol Cell Proteomics. 2013 May;12(5):1180-91. doi: 10.1074/mcp.M112.018846. Epub 2013 Jan 23.
Growth and translation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC toxin.
J Biol Chem. 2012 Apr 13;287(16):12835-47. doi: 10.1074/jbc.M112.340109. Epub 2012 Feb 21.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis.
FEMS Microbiol Lett. 2009 Jan;290(1):45-53. doi: 10.1111/j.1574-6968.2008.01400.x. Epub 2008 Nov 10.
Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes.
Nucleic Acids Res. 2005 Feb 17;33(3):966-76. doi: 10.1093/nar/gki201. Print 2005.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.