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Escherichia coli K-12 substr. MG1655 Protein: SecYEG translocase

Component of: Sec Holo-Translocon (extended summary available)

Subunit composition of SecYEG translocase = [SecE][SecG][SecY]

Summary:
SecE and SecY are inner membrane proteins that are involved in the Sec translocation pathway in E.coli. They were identified as being critical to protein export through interaction with SecA and SecB.

Complementation studies showed that conditional lethal mutations in secY resulted in a defective translocation process [Ito83]. A general defect in protein export is likewise caused by conditional-lethal mutations in the secE locus which also results in an overall increase in SecA transcription as a compensatory action [Riggs88]. Reconstitution of protein translocation has been achieved using purified SecB, SecA, SecY, SecE, a model precursor protein, phospholipids and ATP [Brundage90]. Although SecG is not strictly required for translocation, studies using reconstituted proteoliposomes show that SecG can be indispensable for translocation at 20 degrees but not at 37 degrees, and that SecG is also critical for translocation in the absence of proton motive force [Hanada96]. This cold-sensitive phenotype results from the combination of the secG mutation with a second mutation in glpR [Flower01]. Immunoprecipitation studies show that antiserum against SecY precipitates all three components of the SecYEG complex [Brundage90]. It has also been established that SecY constitutes, at least in part, the channel through which the translocating polypeptide passes across the inner membrane [Joly93].

Escherichia coli SecYEG has been shown to form dimers in membranes. SecYEG has been stabilized with monoclonal antibodies to form dimers in detergent solution [Tziatzios04]. FRET and freeze-fracture analyses indicate the heterotrimeric SecYEG exists in the membrane in an equilibrium of monomers, dimers, and tetramers, which is shifted toward oligomerization by insertion into the membrane of preprotein-bound SecA in the presence of ATP [Scheuring05]. The oligomeric state of the SecYEG complex may be influenced by the substrate that is to be transported [Boy09]. A SecYEG monomer is sufficient for SecA driven protein translocation in vitro [Kedrov11, Taufik13]. The SecYEG dimer binds one substrate polypeptide [Hizlan12]. Two copies of SecY are required for pre-protein transport in vitro [Dalal12].

Purified SecYEG has been incorporated into nanodiscs (soluble lipid bilayer structures of controlled size). Nanodisc reconstituted SecYEG binds monomeric SecA. Acidic lipids in the vicinity of nanodisc reconstituted SecYEG contribute to both SecA binding and ATPase activity [Alami07]. An inner membrane glycolipid, termed membrane protein integrase, modulates the dimer orientation of SecYEG [Moser13]

A medium resolution structure from two-dimensional crystals of E. coli SecYEG has been obtained [Breyton02] along with a higher resolution crystal structure from Methanococcus jannaschii [Van04c]. Together the structures identify a protein conducting channel that is constricted in the centre by a ring of hydrophobic residues (the pore ring) and capped with a short helical domain termed the plug. It has been suggested that these structures may function to seal and close the channel and a 'channel gating' model has been proposed whereby in the resting state the helical plug domain interacts with the pore ring residues and seals the channel while during active translocation the pore domain widens and the plug is displaced (reviewed in [Collinson05]). Studies on the in vivo permeation of small molecules using E. coli plug deletion mutants and pore ring mutants indicate that the SecYEG channel is sealed both in the resting state and when translocating a polypeptide [Park11c]. Structures of active and inactive ribosome-SecYEG channel complexes have been determined using cryo-electron microscopy (cryo-EM). Saliently, ribosome binding per se induces only minor conformational changes to the channel - stable opening of the channel requires loop insertion of the nascent polypeptide with the hydrophobic signal sequence intercalated into the lateral open gate [Park13]

Cryo-EM structures of the SecYEG complex bound to a translating ribosome suggest that two SecYEG heterotrimers constitute the protein conducting channel [Mitra05] and highlight ribosome-lipid interactions and the path of the nascent polypeptide chain from the peptidyltransferase centre within the ribosomal exit tunnel into the protein conducting channel of SecYEG [Frauenfeld11].

FtsY and SecY have been shown to interact in vitro through chemical crosslinking/immunoprecipitation, coimmunoprecipitation, and co-affinity purification studies. This interaction couples signal recognition of membrane proteins to their translocation [Angelini05].

Reviews: [Rusch07, Dalal11]

Citations: [Tam05, Osborne93, Derman93, Nouwen96, Collinson01]

Locations: inner membrane

Relationship Links: PDB:Structure:2AKH , PDB:Structure:2AKI , PDB:Structure:3J00 , PDB:Structure:3J01

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005887 - integral component of plasma membrane Author statement Inferred from experiment [Breyton02, Ito90a]
GO:0031522 - cell envelope Sec protein transport complex Inferred from experiment [Breyton02, Brundage90]

Credits:
Last-Curated ? 09-Oct-2013 by Mackie A , Macquarie University


Subunit of: Sec Holo-Translocon

Synonyms: Sec translocation complex

Subunit composition of Sec Holo-Translocon = [(YidC)(YajC)(SecF)(SecD)][(SecE)(SecG)(SecY)]
         SecD-SecF-YajC-YidC Secretion Complex = (YidC)(YajC)(SecF)(SecD) (extended summary available)
                 inner-membrane protein insertion factor = YidC (extended summary available)
         SecYEG translocase = (SecE)(SecG)(SecY) (extended summary available)

Summary:
The Sec 'holo-translocon' (HTL) is a large multisubunit complex that mediates the transport of nascent polypeptides across, or their integration into, the cytoplasmic membrane. The holo-translocon is a seven subunit complex containing an inner membrane heterotrimeric SecYEG complex that forms the protein conducting channel plus an ancillary complex, SecDFYajC and the Yid C membrane protein, both of which interact with SecYEG to enhance protein transport or integration. The energy for protein translocation is provided by the motor protein ATPase SecA and the proton motive force. The HTL complex is less effective in ATP-dependent SecA-driven protein secretion and more dependent on the PMF [Schulze14].

Simultaneous overexpression of all 7 subunits of the sec HTL facilitates purification and isolation of a complex that is competent for protein secretion and for membrane protein insertion in vitro. The complex contains one copy of SecYEG, one copy of SecDFYajC and one copy of YidC. The HTL associates preferentially with ribosomes displaying nascent peptide. Protein translocation in HTL containing proteoliposomes is stimulated by cardiolipin and by the PMF [Schulze14].

Two pathways of protein translocation converge at the Sec translocon. In the posttranslational pathway the newly synthesised polypeptide is bound by SecB, a cytosolic chaperone which aids targeting to the membrane and maintains a translocation competent conformation of the pre-protein, while in the co-translational pathway the SRP complex binds to the nascent protein as it emerges from the ribosome and the SRP/ribosome/protein complex is then targeted to the Sec translocase.

An experimental approach using alkaline phosphatase (PhoA) fusions to protein signal sequences has allowed discrimination between the major modes of transport, including the Sec protein translocase, across the inner membrane [Marrichi08].

Reviews: [Lycklama12, duPlessis11, Driessen08, Driessen98, deKeyzer03, Manting00, Gold07].
Comments: [Duong14]

Citations: [Ojemalm13]

Molecular Weight: 250.0 kD (experimental) [Schulze14]

GO Terms:

Biological Process: GO:0043952 - protein transport by the Sec complex Inferred from experiment [Schulze14]
GO:0065002 - intracellular protein transmembrane transport Inferred from experiment [Schulze14]
Molecular Function: GO:0009977 - proton motive force dependent protein transmembrane transporter activity Inferred from experiment [Schulze14]
GO:0015462 - protein-transmembrane transporting ATPase activity Inferred from experiment [Schulze14]
Cellular Component: GO:0031522 - cell envelope Sec protein transport complex Inferred from experiment [Schulze14]

Credits:
Last-Curated ? 06-Jul-2014 by Mackie A , Macquarie University


Subunit of SecYEG translocase: SecE

Synonyms: MbrC, PrlG

Gene: secE Accession Numbers: EG10939 (EcoCyc), b3981, ECK3972

Locations: inner membrane

Sequence Length: 127 AAs

Molecular Weight: 13.643 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006886 - intracellular protein transport Inferred from experiment [Riggs88]
GO:0043952 - protein transport by the Sec complex Inferred from experiment Inferred by computational analysis [GOA06, Riggs88]
GO:0065002 - intracellular protein transmembrane transport Inferred from experiment Inferred by computational analysis [GOA06, Riggs88]
GO:0006605 - protein targeting Inferred by computational analysis [GOA06, GOA01]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0009306 - protein secretion Inferred by computational analysis [GOA06, GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0008565 - protein transporter activity Inferred by computational analysis [GOA06]
GO:0015450 - P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005622 - intracellular Inferred by computational analysis Inferred from experiment [Riggs88, GOA06]
GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, DiazMejia09, Zhang07, Daley05, Schatz89]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Schatz89]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Homma97, Schatz89]
GO:0031522 - cell envelope Sec protein transport complex Inferred from experiment [Brundage90]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]

MultiFun Terms: cell structure membrane
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The Type II (General) Secretory Pathway (IISP) Family

Unification Links: DIP:DIP-59303N , EcoliWiki:b3981 , PR:PRO_000023926 , Pride:P0AG96 , Protein Model Portal:P0AG96 , RefSeq:NP_418408 , SMR:P0AG96 , String:511145.b3981 , UniProt:P0AG96

Relationship Links: InterPro:IN-FAMILY:IPR001901 , InterPro:IN-FAMILY:IPR005807 , PDB:Structure:2AKH , PDB:Structure:2AKI , PDB:Structure:3J01 , Pfam:IN-FAMILY:PF00584 , Prints:IN-FAMILY:PR01650 , Prosite:IN-FAMILY:PS01067

Summary:
SecE is an inner membrane protein involved in the Sec secretion pathway.

Sub-proteomic analysis of cells lacking SecE indicates that several secretory and inner membrane proteins are able to utilise Sec translocon-independent pathways or access remaining Sec translocons in these SecE-depleted cells [Baars08].

Essentiality data for secE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 2]

Subunit of SecYEG translocase: SecG

Synonyms: PrlH

Gene: secG Accession Numbers: EG12095 (EcoCyc), b3175, ECK3164

Locations: inner membrane

Sequence Length: 110 AAs

Molecular Weight: 11.365 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006886 - intracellular protein transport Inferred from experiment [Douville95]
GO:0043952 - protein transport by the Sec complex Inferred from experiment [Brundage90, Douville95]
GO:0065002 - intracellular protein transmembrane transport Inferred from experiment [Douville95]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Karamanou08]
GO:0015450 - P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005622 - intracellular Inferred from experiment [Douville95]
GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Douville95]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01]

MultiFun Terms: cell structure membrane
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The Type II (General) Secretory Pathway (IISP) Family

Unification Links: DIP:DIP-47480N , EcoliWiki:b3175 , Mint:MINT-6477974 , PR:PRO_000023928 , Pride:P0AG99 , Protein Model Portal:P0AG99 , RefSeq:NP_417642 , SMR:P0AG99 , String:511145.b3175 , UniProt:P0AG99

Relationship Links: InterPro:IN-FAMILY:IPR004692 , PDB:Structure:2AKH , PDB:Structure:2AKI , Pfam:IN-FAMILY:PF03840 , Prints:IN-FAMILY:PR01651

Summary:
SecG is an inner membrane protein involved in the Sec protein secretion pathway.

Essentiality data for secG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 3]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 4]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 3]

Subunit of SecYEG translocase: SecY

Synonyms: PrlA

Gene: secY Accession Numbers: EG10766 (EcoCyc), b3300, ECK3287

Locations: inner membrane

Sequence Length: 443 AAs

Molecular Weight: 48.512 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006886 - intracellular protein transport Inferred from experiment [Baba90]
GO:0043952 - protein transport by the Sec complex Inferred from experiment Inferred by computational analysis [GOA06, Shiba84, Brundage90, Baba90]
GO:0065002 - intracellular protein transmembrane transport Inferred from experiment Inferred by computational analysis [GOA06, Baba90]
GO:0006605 - protein targeting Inferred by computational analysis [GOA06]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Karamanou08, Snyders97]
Cellular Component: GO:0005622 - intracellular Inferred by computational analysis Inferred from experiment [Baba90, GOA06]
GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, DiazMejia09, Zhang07, Daley05, Akiyama85]
GO:0005887 - integral component of plasma membrane Author statement Inferred from experiment [Watanabe89b, Ito90a]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Akiyama85]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]

MultiFun Terms: cell structure membrane
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The Type II (General) Secretory Pathway (IISP) Family

Unification Links: DIP:DIP-59302N , EcoliWiki:b3300 , ModBase:P0AGA2 , PR:PRO_000023930 , Pride:P0AGA2 , Protein Model Portal:P0AGA2 , RefSeq:NP_417759 , SMR:P0AGA2 , String:511145.b3300 , UniProt:P0AGA2

Relationship Links: InterPro:IN-FAMILY:IPR002208 , InterPro:IN-FAMILY:IPR023201 , InterPro:IN-FAMILY:IPR026593 , Panther:IN-FAMILY:PTHR10906 , PDB:Structure:2AKH , PDB:Structure:2AKI , PDB:Structure:3J01 , Pfam:IN-FAMILY:PF00344 , Prosite:IN-FAMILY:PS00755 , Prosite:IN-FAMILY:PS00756

Summary:
SecY is required for efficient protein translocation across the cytoplasmic membrane [Shiba84, Ito84, Ito83, Baba90]. It is one of three integral membrane proteins comprising the SecYEG translocation apparatus. SecY is believed to be the channel through which the translocating polypeptide passes through across the inner membrane [Joly93]. SecY binds synthetic signal peptide in vitro [Wang04e].

SecY contains 10 transmembrane domains, 5 periplasmic domains and 6 cytosolic domains. The N and C-termini are located in the cytoplasm [Akiyama87]

Review: [Ito90a]

Citations: [Robson09, Watanabe89b, Baba94, Veenendaal01, vanderSluis02, Shimokawa03, Satoh03, Satoh03a]

Essentiality data for secY knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 2]

References

Akiyama85: Akiyama Y, Ito K (1985). "The SecY membrane component of the bacterial protein export machinery: analysis by new electrophoretic methods for integral membrane proteins." EMBO J 4(12);3351-6. PMID: 3004955

Akiyama87: Akiyama Y, Ito K (1987). "Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli." EMBO J 6(11);3465-70. PMID: 2828030

Alami07: Alami M, Dalal K, Lelj-Garolla B, Sligar SG, Duong F (2007). "Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA." EMBO J 26(8);1995-2004. PMID: 17396152

Angelini05: Angelini S, Deitermann S, Koch HG (2005). "FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon." EMBO Rep 6(5);476-81. PMID: 15815684

Baars08: Baars L, Wagner S, Wickstrom D, Klepsch M, Ytterberg AJ, van Wijk KJ, de Gier JW (2008). "Effects of SecE depletion on the inner and outer membrane proteomes of Escherichia coli." J Bacteriol 190(10);3505-25. PMID: 18296516

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

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Baba94: Baba T, Taura T, Shimoike T, Akiyama Y, Yoshihisa T, Ito K (1994). "A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex." Proc Natl Acad Sci U S A 91(10);4539-43. PMID: 8183945

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Lycklama12: Lycklama A Nijeholt JA, Driessen AJ (2012). "The bacterial Sec-translocase: structure and mechanism." Philos Trans R Soc Lond B Biol Sci 367(1592);1016-28. PMID: 22411975

Manting00: Manting EH, Driessen AJ (2000). "Escherichia coli translocase: the unravelling of a molecular machine." Mol Microbiol 37(2);226-38. PMID: 10931320

Marrichi08: Marrichi MJ, Camacho L, Russell DG, Delisa MP (2008). "Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria." J Biol Chem 283(50):35223-35. PMID: 18819916

Mitra05: Mitra K, Schaffitzel C, Shaikh T, Tama F, Jenni S, Brooks CL, Ban N, Frank J (2005). "Structure of the E. coli protein-conducting channel bound to a translating ribosome." Nature 438(7066);318-24. PMID: 16292303

Moser13: Moser M, Nagamori S, Huber M, Tokuda H, Nishiyama K (2013). "Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation." Proc Natl Acad Sci U S A 110(24);9734-9. PMID: 23716687

Nouwen96: Nouwen N, de Kruijff B, Tommassen J (1996). "prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors." Proc Natl Acad Sci U S A 93(12);5953-7. PMID: 8650200

Ojemalm13: Ojemalm K, Botelho SC, Studle C, von Heijne G (2013). "Quantitative analysis of SecYEG-mediated insertion of transmembrane α-helices into the bacterial inner membrane." J Mol Biol 425(15);2813-22. PMID: 23659793

Osborne93: Osborne RS, Silhavy TJ (1993). "PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains." EMBO J 12(9);3391-8. PMID: 8253067

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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