| Primary Identifier | IPR010263 | Type | Family |
| Short Name | T6SS_TssK |
| description | TssK is an essential baseplate component of the type VI secretion system, which connects the membrane complex, the baseplate and the tail components [, , ].The structure of TssK was solved revealing the proteins organise into a tightly packed trimer [, ]. Each TssK monomer comprises three domains: an N-terminal β-sandwich domain, a linker and a four-helix-bundle middledomain, and a C-terminal domain. The N-terminal domain of TssK is structurally homologous to the shoulder domain of phage receptor-binding proteins, and the C-terminal domain binds the T6SS membrane complex [].This family includes TssK proteins and TssK homologues ImpJ and vasE.The type VI secretion system (T6SS) is a supra-molecular bacterial complex that resembles phage tails. It is a toxin delivery systems which fires toxins into target cells upon contraction of its TssBC sheath []. Thirteen essential core proteins are conserved in all T6SSs: the membrane associated complex TssJ-TssL-TssM, the baseplate proteins TssE, TssF, TssG, and TssK, the bacteriophage-related puncturing complex composed of the tube (Hcp), the tip/puncturing device VgrG, and the contractile sheath structure (TssB and TssC). Finally, the starfish-shaped dodecameric protein, TssA, limits contractile sheath polymerization at its distal part when TagA captures TssA []. |
