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). acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein] Is potently inhibited by several small-molecule that share an isothiazole S,S-dioxide heterocyclic core. Some of these inhibitors, when used in combination with KAN against resistant M.tuberculosis, efficiently overcome Eis-mediated KAN resistance by restoring the antibacterial activity of KAN. kcat is 0.020 sec(-1) with amikacin as substrate. kcat is 0.039 sec(-1) with kanamycin as substrate. kcat is 0.070 sec(-1) with neamine as substrate. kcat is 0.130 sec(-1) with neomycin B as substrate. kcat is 0.482 sec(-1) with netilmicin as substrate. kcat is 0.058 sec(-1) with paromomycin as substrate. kcat is 0.270 sec(-1) with sisomicin as substrate. kcat is 0.162 sec(-1) with tobramycin as substrate (at 25 degrees Celsius and pH 8.0) (PubMed:21628583). kcat is 0.017 sec(-1) with amikacin as substrate. kcat is 0.032 sec(-1) with kanamycin A as substrate. kcat is 0.032 sec(-1) with paromomycin as substrate. kcat is 0.179 sec(-1) with tobramycin as substrate (at 25 degrees Celsius and pH 8.0) (PubMed:22547814). kcat is 1.25 sec(-1) with capreomycin as substrate (at 25 degrees Celsius and pH 8.0) (PubMed:23233486). Catalytic efficiency is 3-fold higher for acetylation of kanamycin than for acetylation of amikacin (PubMed:19906990). Homohexamer; trimer of dimers. Eis is present in the macrophage cytoplasm from 4 to 96 hours post-infection. The Eis monomer consists of three regions that are assembled into a heart-shaped molecule (PubMed:21628583). This shape is formed by an unusual fusion of two general control non-derepressible 5 (GCN5)-related N-acetyltransferase (GNAT) regions and a C-terminal region (PubMed:21628583). The N-acetyltransferase domain of Eis is responsible for its modulation of ROS generation and pro-inflammatory responses in macrophages (PubMed:21187903). No significant difference in terms of intracellular survival in U-397 macrophages and in an in vivo mouse aerosol model of infection (PubMed:17259625). A strain lacking this gene induces more TNF-alpha but less IL-10 production in primary human monocytes than wild-type (PubMed:17259625). Macrophages infected with a M.tuberculosis eis-deletion mutant display markedly increased accumulation of massive autophagic vacuoles and formation of autophagosomes in vitro and in vivo (PubMed:21187903). Infection of macrophages with this mutant increases the production of tumor necrosis factor-alpha and interleukin-6 over the levels produced by infection with wild-type or complemented strains (PubMed:21187903). Elevated ROS generation in macrophages infected with this mutant (for which NADPH oxidase and mitochondria are largely responsible) render the cells highly sensitive to autophagy activation and cytokine production; despite considerable activation of autophagy and pro-inflammatory responses, these infected macrophages undergo caspase-independent cell death (PubMed:21187903). Increased expression of eis due to point mutations in the promoter region of eis is responsible for resistance to the second-line injectable drug kanamycin in a number of M.tuberculosis clinical isolates, through acetylation of its amino groups, which leads to inactivation of the drug. Belongs to the acetyltransferase Eis family. Truncated N-terminus.