LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component [ ]. From there, the mature proteins are either targeted to the outer membrane, or remain as periplasmic proteins. The translocase protein subunits are encoded on the bacterial chromosome. The translocase itself comprises 7 proteins, including a chaperone protein (SecB), an ATPase (SecA), an integral membrane complex (SecCY, SecE and SecG), and two additional membrane proteins that promote the release of the mature peptide into the periplasm (SecD and SecF) [ ]. The chaperone protein SecB [] is a highly acidic homotetrameric protein that exists as a "dimer of dimers"in the bacterial cytoplasm. SecB maintains preproteins in an unfolded state after translation, and targets these to the peripheral membrane protein ATPase SecA for secretion []. Together with SecY and SecG, SecE forms a multimeric channel through which preproteins are translocated, using both proton motive forces and ATP-driven secretion. The latter is mediated by SecA. The structure of the Escherichia coli SecYEG assembly revealed a sandwich of two membranesinteracting through the extensive cytoplasmic domains [ ]. Each membrane is composed of dimers of SecYEG. Themonomeric complex contains 15 transmembrane helices. This entry describes the SecD family of transport proteins, which are parts of the Sec protein translocase complex. Members of this family are highly variable in length immediately after the well-conserved motif LGLGLXGG at the amino-terminal end of this model. Archaeal homologues are not included in the seed. SecD from Mycobacterium tuberculosis has a long Pro-rich insert. SecD interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA [ ]. |
| Short Name | SecD |
