SecY protein

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eubacterial secY protein
Identifiers
Symbol SecY
Pfam PF00344
InterPro IPR002208
PROSITE PDOC00612
SCOP 1rh5
TCDB 3.A.5
OPM family 19
OPM protein 1rh5
Available PDB structures:

1rh5A:69-417 1rhzA:69-417

SecY protein is main transmembrane subunit of eubacterial protein secretory pathway and protein-secreting ATPase complex, also known as translocon.

Secretion across the inner membrane in 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.[1]. 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 pathway 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)[1]. The chaperone protein SecB[2] 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[3]. The structure of the Escherichia coli SecYEG assembly revealed a sandwich of two membranes interacting through the extensive cytoplasmic domains[4]. Each membrane is composed of dimers of SecYEG. The monomeric complex contains 15 transmembrane helices.

The eubacterial secY protein[5] interacts with the signal sequences of secretory proteins as well as with two other components of the protein translocation system: secA and secE. SecY is an integral plasma membrane protein of 419 to 492 amino acid residues that apparently contains 10 transmembrane (TM), 6 cytoplasmic and 5 periplasmic regions.

Cytoplasmic regions 2 and 3, and TM domains 1, 2, 4, 5, 7 and 10 are well conserved: the conserved cytoplasmic regions are believed to interact with cytoplasmic secretion factors, while the TM domains may participate in protein export[6]. Homologs of secY are found in archaebacteria[7]. SecY is also encoded in the chloroplast genome of some algae[8] where it could be involved in a prokaryotic-like protein export system across the two membranes of the chloroplast endoplasmic reticulum (CER) which is present in chromophyte and cryptophyte algae.

[edit] Subfamilies

[edit] Human proteins containing this domain

SEC61A1; SEC61A2;

[edit] References

  1. ^ a b Bieker KL, Phillips GJ, Silhavy TJ (1990). "The sec and prl genes of Escherichia coli". J. Bioenerg. Biomembr. 22 (3): 291–310. PMID 2202721. 
  2. ^ Driessen AJ (2001). "SecB, a molecular chaperone with two faces". Trends Microbiol. 9 (5): 193–196. doi:10.1016/S0966-842X(01)01980-1. PMID 11336818. 
  3. ^ Muller JP (1999). "Effects of pre-protein overexpression on SecB synthesis in Escherichia coli". FEMS Microbiol. Lett. 176 (1): 219–227. PMID 10418149. 
  4. ^ Rapoport TA, Breyton C, Haase W, Kuhlbrandt W, Collinson I (2002). "Three-dimensional structure of the bacterial protein-translocation complex SecYEG". Nature 418 (6898): 662–665. doi:10.1038/nature00827. PMID 12167867. 
  5. ^ Ito K (1992). "SecY and integral membrane components of the Escherichia coli protein translocation system". Mol. Microbiol. 6 (17): 2423–2428. PMID 1406280. 
  6. ^ Oliver DB, Suh JW, Thomas SM, Dolan KM, Price CW, Boylan SA (1990). "Isolation of a secY homologue from Bacillus subtilis: evidence for a common protein export pathway in eubacteria". Mol. Microbiol. 4 (2): 305–314. doi:10.1111/j.1365-2958.1990.tb00597.x. PMID 2110998. 
  7. ^ Auer J, Spicker G, Bock A (1991). "Presence of a gene in the archaebacterium Methanococcus vannielii homologous to secY of eubacteria". Biochimie 73 (6): 683–688. doi:10.1016/0300-9084(91)90048-6. PMID 1764515. 
  8. ^ Douglas SE (1992). "A secY homologue is found in the plastid genome of Cryptomonas phi". FEBS Lett. 298 (1): 93–96. doi:10.1016/0014-5793(92)80029-G. PMID 1544427. 
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