Rv1794



Type
protein_coding
Name
Rv1794
Locus Name

Rv1794

Product

Conserved protein

Functional Category

Conserved hypotheticals

Location
2031066..2031968 (+ strand)
Gene Length
902 bp
Nucleotides
TGGATCAACAGAGTACCCGCACCGACATCACCGTCAACGTCGACGGCTTCTGGATGCTTCAGGCGCTACTGGATATCCGCCACGTTGCGCCTGAGTTACGTTGCCGGCCGTACGTCTCCACCGATTCCAATGACTGGCTAAACGAGCACCCGGGGATGGCGGTCATGCGCGAGCAGGGCATTGTCGTCAACGACGCGGTCAACGAACAGGTCGCTGCCCGGATGAAGGTGCTTGCCGCACCTGATCTTGAAGTCGTCGCCCTGCTGTCACGCGGCAAGTTGCTGTACGGGGTCATAGACGACGAGAACCAGCCGCCGGGTTCGCGTGACATCCCTGACAATGAGTTCCGGGTGGTGTTGGCCCGGCGAGGCCAGCACTGGGTGTCGGCGGTACGGGTTGGCAATGACATCACCGTCGATGACGTGACGGTCTCGGATAGCGCCTCGATCGCCGCACTGGTAATGGACGGTCTGGAGTCGATTCACCACGCCGACCCAGCCGCGATCAACGCGGTCAACGTGCCAATGGAGGAGATGCTAGAGGCAACGAAGTCGTGGCAGGAATCGGGGTTTAACGTCTTCTCCGGCGGAGATCTGCGCCGAATGGGCATCAGTGCCGCGACGGTGGCCGCGCTGGGGCAGGCGTTGTCGGATCCCGCGGCCGAGGTCGCAGTGTATGCGCGACAGTACCGAGACGACGCCAAGGGCCCCAGCGCCTCGGTGTTGTCGCTGAAAGACGGCTCCGGTGGACGCATCGCGCTGTATCAGCAGGCGCGAACGGCAGGTTCCGGCGAGGCGTGGCTGGCTATCTGCCCGGCTACCCCGCAGTTGGTGCAAGTAGGAGTGAAGACCGTTTTGGATACACTGCCCTACGGCGAGTGGAAAACACACAGCAGAGTATGA
Drug Resistance

Check for drug resistance association at TBDREAMDB

Mutations

Check for mutants available at TARGET


Function
Specific chaperone for cognate PE/PPE proteins. Plays an important role in preventing aggregation of PE/PPE dimers. {ECO:0000269|PubMed:25155747}.
Family

EspG family

GO
InterPro

UniProt
O53943
GenBank
Rv1794
EnsemblBacteria
Rv1794
Mycobrowser
Rv1794


4KXR
Summary
Name
ESX-5 secretion-associated protein EspG5
Family
EspG family
Protein Sequence
MDQQSTRTDITVNVDGFWMLQALLDIRHVAPELRCRPYVSTDSNDWLNEHPGMAVMREQGIVVNDAVNEQVAARMKVLAAPDLEVVALLSRGKLLYGVIDDENQPPGSRDIPDNEFRVVLARRGQHWVSAVRVGNDITVDDVTVSDSASIAALVMDGLESIHHADPAAINAVNVPMEEMLEATKSWQESGFNVFSGGDLRRMGISAATVAALGQALSDPAAEVAVYARQYRDDAKGPSASVLSLKDGSGGRIALYQQARTAGSGEAWLAICPATPQLVQVGVKTVLDTLPYGEWKTHSRV
Mass
32,400 Da
Length
300 Aa

Rv1794 doesn't seem to be a targeted by any drug.


Rv1794 doesn't seem to be involved in any pathway.


Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion.
Proc Natl Acad Sci U S A. 2014 Oct 14;111(41):14758-63. doi: 10.1073/pnas.1409345111. Epub 2014 Oct 1.
Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG5 in complex with PE25-PPE41 dimer.
Mol Microbiol. 2014 Oct;94(2):367-82. doi: 10.1111/mmi.12770. Epub 2014 Sep 15.
Disruption of the ESX-5 system of Mycobacterium tuberculosis causes loss of PPE protein secretion, reduction of cell wall integrity and strong attenuation.
Mol Microbiol. 2012 Mar;83(6):1195-209. doi: 10.1111/j.1365-2958.2012.08001.x. Epub 2012 Feb 20.
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.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.