- SecY protein
Pfam_box
Symbol = SecY
Name = eubacterial secY protein
width =
caption =
Pfam= PF00344
InterPro= IPR002208
SMART=
PROSITE = PDOC00612
SCOP = 1rh5
TCDB = 3.A.5
OPM family= 19
OPM protein= 1rh5
PDB=PDB3|1rh5A:69-417 PDB3|1rhzA:69-417SecY protein is main transmembrane subunit of eubacterial protein
secretory pathway andprotein-secreting ATPase complex, also known astranslocon .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.cite journal |author=Bieker KL, Phillips GJ, Silhavy TJ |title=The sec and prl genes of Escherichia coli |journal=J. Bioenerg. Biomembr. |volume=22 |issue=3 |pages=291–310 |year=1990 |pmid=2202721] . 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). The chaperone protein SecBcite journal |author=Driessen AJ |title=SecB, a molecular chaperone with two faces |journal=Trends Microbiol. |volume=9 |issue=5 |pages=193–196|year=2001 |pmid=11336818 |doi=10.1016/S0966-842X(01)01980-1] 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 secretioncite journal |author=Muller JP |title=Effects of pre-protein overexpression on SecB synthesis in Escherichia coli |journal=FEMS Microbiol. Lett. |volume=176 |issue=1 |pages=219–227 |year=1999 |pmid=10418149] . The structure of the Escherichia coli SecYEG assembly revealed a sandwich of two membranes interacting through the extensive cytoplasmic domainscite journal |author=Rapoport TA, Breyton C, Haase W, Kuhlbrandt W, Collinson I |title=Three-dimensional structure of the bacterial protein-translocation complex SecYEG |journal=Nature |volume=418 |issue=6898 |pages=662–665 |year=2002 |pmid=12167867 |doi=10.1038/nature00827] . Each membrane is composed of dimers of SecYEG. The monomeric complex contains 15 transmembrane helices.The eubacterial secY proteincite journal |author=Ito K |title=SecY and integral membrane components of the Escherichia coli protein translocation system |journal=Mol. Microbiol. |volume=6 |issue=17 |pages=2423–2428 |year=1992 |pmid=1406280] interacts with the signal sequences of secretory proteins as well as with two other components ofthe 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 exportcite journal |author=Oliver DB, Suh JW, Thomas SM, Dolan KM, Price CW, Boylan SA |title=Isolation of a secY homologue from Bacillus subtilis: evidence for a common protein export pathway in eubacteria |journal=Mol. Microbiol. |volume=4 |issue=2 |pages=305–314 |year=1990 |pmid=2110998 |doi=10.1111/j.1365-2958.1990.tb00597.x] . Homologs of secY are found in archaebacteriacite journal |author=Auer J, Spicker G, Bock A |title=Presence of a gene in the archaebacterium Methanococcus vannieliihomologous to secY of eubacteria |journal=Biochimie |volume=73 |issue=6 |pages=683–688 |year=1991 |pmid=1764515 |doi=10.1016/0300-9084(91)90048-6] . SecY is also encoded in the chloroplast genome of some algaecite journal |author=Douglas SE |title=A secY homologue is found in the plastid genome of Cryptomonas phi |journal=FEBS Lett. |volume=298 |issue=1 |pages=93–96 |year=1992 |pmid=1544427 |doi=10.1016/0014-5793(92)80029-G] 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.
ubfamilies
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SecY-related translocase InterPro|IPR014269Human proteins containing this domain
SEC61A1 ;SEC61A2 ;References
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