The SRP signal sequence of KdpD.

ABSTRACT: KdpD is a four-spanning membrane protein that has two large cytoplasmic domains at the amino- and at the carboxyterminus, respectively. During its biogenesis KdpD binds to the signal recognition particle (SRP) of Escherichia coli that consists of a 48-kDa protein Ffh and a 4.5S RNA. The protein is targeted to the inner membrane surface and is released after contacting the SRP receptor protein FtsY. The information within the KdpD protein that confers SRP interaction was found in the amino-terminal cytoplasmic domain of KdpD, particularly at residues 22-48. Within this sequence a Walker A motif is present at residues 30-38. To determine the actual sequence specificity to SRP, a collection of mutants was constructed. When the KdpD peptides (residues 22-48) were fused to sfGFP the targeting t

SUBMITTER: Pross E 

PROVIDER: S-EPMC6581901 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature