| Description | T6SS bacteria employ toxic effectors to inhibit rival cells and concurrently use effector cognate immunity proteins to protect their sibling cells. The effector and immunity pairs (E-I pairs) endow the bacteria with a great advantage in niche competition. This is the C-terminal domain of Tli4 (PA1509 in Pseudomonas aeruginosa). The Tle cognate immunity proteins (Tlis) can directly disable the transported Tle protein and thereby mediate the self-protection process. The Tle-Tli effector-immunity (E-I) pairs confer substantial advantage to the donor cell during interbacterial competition. Tli4 displays a two-domain conformation (domains I and II) and contains 17 β-strands and four helices. These two domains pack into a crab claw-like conformation functioning as an inhibitor of Tle4. Both domains adopt an α+β architecture. Domain I features a central antiparallel β-sheet sandwiched by two helices and a short antiparallel β-sheet. This entry comprises the N-terminal domain I found in Tli4 proteins [ ]. | Name | Tle cognate immunity protein 4, N-terminal domain |
| Short Name | Tli4_N | Type | Domain |
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