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eis (P9WFK7) - Overview - Molecular Target Synopsis

Protein


eis, N-acetyltransferase Eis
Enzyme Classification 2.3.1.-
UniProt P9WFK7

Also Known as EIS_MYCTU, eis

Effector that is released into the host cell and affects host immune responses; it negatively modulates inflammation, macrophage autophagy, and cell death through redox-dependent signaling (PubMed:17259625, PubMed:21187903). Acts as an acetyltransferase. Acetylates 'Lys-55' of dual-specificity protein phosphatase 16 (DUSP16)/mitogen-activated protein kinase phosphatase-7 (MKP-7), a JNK-specific phosphatase; this leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS (reactive oxygen species) generation for enhanced intracellular survival of M.tuberculosis (PubMed:22547814). Inhibits Con A-mediated T-cell proliferation in vitro (PubMed:17449476). Treatment of T-cells with Eis inhibits ERK1/2, JAK pathway, and subsequent production of tumor necrosis factor-alpha (TNF-alpha) and interleukin-4 (IL-4); on the contrary, there is increased production of interferon-gamma (IFN-gamma) and interleukin-10 (IL-10), which indicates that immunity in response to Eis treatment is skewed away from a protective T(H)1 response and Eis disturbs the cross regulation of T-cells (PubMed:17449476). When expressed in M.smegmatis, enhances intracellular survival of the bacteria in host macrophages during infection (PubMed:10629183)., Can also acetylate multiple amine groups of many aminoglycoside (AG) antibiotics, leading to their inactivation, and thus contributes to drug resistance (PubMed:19906990, PubMed:21628583, PubMed:24106131). Is also able to acetylate and deactivate the cyclic peptide antibiotic capreomycin, but not the other anti-tuberculous drugs isoniazid and pyrazinamide (PubMed:23233486). Acetylates kanamycin (KAN) more efficiently than amikacin (AMK), even though Eis seems to bind AMK with higher affinity (PubMed:19906990). Does not acetylate and inactivate streptomycin, apramycin and spectinomycin (PubMed:19906990, PubMed:21628583). Homohexamer; trimer of dimers.

6B3T
CRYSTAL STRUCTURE OF ACETYLTRANSFERASE EIS FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH A 1,2,4-TRIAZINO[5,6B]INDOLE-3-THIOETHER INHIBITOR ANALOGUE 39B
RCSB/PDB
Inspect Structure
See all 3D Structures for eis

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform

Sub-cellular localization


UniProt: eis is active in the following subcellular-locations: bacterial extracellular vesicle, extracellular vesicle, host cytoplasmic vesicle, host extracellular space, host phagosome, secreted.
GO terms: eis is active in the following subcellular-locations: bacterial extracellular vesicle, extracellular space of host, host cell cytoplasmic vesicle.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project eis has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For eis there are:
10 structures (29 chains) solved
8 are solved in complex with at least one small molecule ligand
1 are solved with an approved drug

eis is solved in complex with the approved drug(s):

TOY/TOBRAMYCIN (4JD6_A, 4JD6_B).

(see details)
Molecular Target 3D Synopsis