The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase in <i>Vibrio cholerae</i>.

ABSTRACT: Vibrio cholerae secretes a variety of effector proteins that are freely released into the extracellular space via its Type II Secretion System (T2SS) including cholera toxin, the causative agent of the disease cholera. In contrast to cholera toxin, a growing number of T2SS effectors is increasingly understood to remain associated with the cell surface. The serine protease VesB from V. cholerae is a surface protein that is produced with a short C-terminal motif, called GlyGly-CTERM. This motif is linked to the rest of VesB via a predicted unstructured linker. In addition to VesB, V. cholerae encodes five additional GlyGly-CTERM proteins including the serine proteases VesA and VesC, a putative metalloprotease VCA0065, the DNase Xds, and VC1485, a protein of unknown funct

SUBMITTER: Roberts CS 

PROVIDER: S-EPMC12889589 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature