ppa



Type
protein_coding
Name
ppa
Locus Name

Rv3628

Product

Inorganic pyrophosphatase Ppa (pyrophosphate phospho-hydrolase) (PPASE) (inorganic diphosphatase) (diphosphate phospho-hydrolase)

Functional Category

Intermediary metabolism and respiration

Location
4067423..4067911 (+ strand)
Gene Length
488 bp
Nucleotides
TGCAATTCGACGTGACCATCGAAATTCCCAAGGGCCAGCGCAACAAATACGAGGTCGACCATGAGACGGGGCGGGTTCGTCTGGACCGGTACCTGTACACCCCGATGGCCTACCCGACCGACTACGGCTTCATCGAGGACACCCTAGGTGACGATGGCGACCCGCTGGACGCGCTGGTGCTGCTACCGCAGCCGGTCTTCCCCGGGGTGCTGGTGGCGGCGCGGCCGGTGGGGATGTTCCGGATGGTCGACGAGCACGGCGGCGACGACAAAGTGCTGTGCGTCCCAGCCGGTGACCCCCGGTGGGACCACGTCCAAGACATCGGGGACGTTCCGGCTTTCGAGCTGGATGCGATCAAGCATTTCTTTGTGCACTACAAGGACCTGGAACCAGGTAAGTTCGTCAAGGCGGCCGACTGGGTCGACCGCGCCGAAGCCGAGGCAGAGGTGCAGCGTTCAGTGGAGCGCTTCAAGGCCGGTACACACTGA
Drug Resistance

Check for drug resistance association at TBDREAMDB

Mutations

Check for mutants available at TARGET


Function
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000269|PubMed:16239227, ECO:0000269|PubMed:26296329}.; FUNCTION: Antigen that activates dendritic cells (DCs), increasing their expression of cell surface molecules and augmenting their production of TNF-alpha, IL-1beta, IL-6, IL-23 and IL-12p70. Rv3628 mediates these effects by binding to TLR2 and activating downstream MyD88-, MAPK- and NF-kappaB-dependent signaling pathways. Rv3628-stimulated DCs induce the expansion of OVA-specific CD4+ and CD8+ T cells which secrete IFN-gamma and IL-2, and the generation of effector/memory T cells. Thus, Rv3628 polarizes DCs toward a Th1 immune response and promotes protective immunity against M.tuberculosis infection. Is not able to bind to TLR4 molecules on the cell surface. {ECO:0000269|PubMed:27097115}.
Family

PPase family

GO
InterPro

UniProt
P9WI55
GenBank
Rv3628
EnsemblBacteria
Rv3628
Mycobrowser
Rv3628


1SXV
Summary
Name
Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase)
Family
PPase family
Protein Sequence
MQFDVTIEIPKGQRNKYEVDHETGRVRLDRYLYTPMAYPTDYGFIEDTLGDDGDPLDALVLLPQPVFPGVLVAARPVGMFRMVDEHGGDDKVLCVPAGDPRWDHVQDIGDVPAFELDAIKHFFVHYKDLEPGKFVKAADWVDRAEAEAEVQRSVERFKAGTH
Mass
18,329 Da
Length
162 Aa

Rv3628 doesn't seem to be a targeted by any drug.



Structural and computational dissection of the catalytic mechanism of the inorganic pyrophosphatase from Mycobacterium tuberculosis.
J Struct Biol. 2015 Oct;192(1):76-87. doi: 10.1016/j.jsb.2015.08.010. Epub 2015 Aug 19.
Structure of the Mycobacterium tuberculosis soluble inorganic pyrophosphatase Rv3628 at pH 7.0.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):866-70. doi: 10.1107/S1744309111023323. Epub 2011 Jul 26.
An unusual, His-dependent family I pyrophosphatase from Mycobacterium tuberculosis.
J Biol Chem. 2005 Dec 23;280(51):41819-26. doi: 10.1074/jbc.M509489200. Epub 2005 Oct 20.
Mycobacterium tuberculosis Rv3628 drives Th1-type T cell immunity via TLR2-mediated activation of dendritic cells and displays vaccine potential against the hyper-virulent Beijing K strain.
Oncotarget. 2016 May 3;7(18):24962-82. doi: 10.18632/oncotarget.8771.
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.
Analysis of stress- and host cell-induced expression of the Mycobacterium tuberculosis inorganic pyrophosphatase.
BMC Microbiol. 2001;1:3. Epub 2001 Apr 24.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.