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Escherichia coli K-12 substr. MG1655 Protein: 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 ]

Gene-Reaction Schematic: ?

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 Sec Holo-Translocon: SecD-SecF-YajC-YidC Secretion Complex

Summary:
SecD/SecF/YajC and YidC are all components of the Sec protein secretion pathway. They are believed to work in conjunction with SecYEG to stabilize the insertion of SecA and its bound preprotein into the inner membrane.

In studies of conditional lethal mutations of secD and secF genes, secA transcription was found to be stimulated due to severe general protein translocation defects. Deletions of secD result in cold-sensitive mutations which could be complemented by plasmids containing the gene [Gardel87]. Overexpression of SecD and SecF increases translocation in wild-type cells [Pogliano94]. Within the same operon as secD and secF is a third gene known as yajC which may also have a role in protein translocation [Pogliano94a]. Co-purification studies [Samuelson00] indicate that YidC is associated with the SecYEG translocase complex and plays a role in the assembly of inner membrane proteins. Subsequent studies [Nouwen02] show that, under conditions of SecD/SecF/YajC overproduction, YidC forms a heterotetrameric complex with SecD/SecF/YajC.

In vitro reconstitution studies demonstrated that the presence of SecD/SecF/YajC stabilizes the SecA insertion complex and inhibits movement of the SecA bound precursor in either direction [Duong97]. If this model holds true, then the SecD/SecF/YajC/YidC stabilization complex must be released from the SecYEG complex or be otherwise inactivated in order for SecA to de-insert from the complex and to begin another round of stepwise translocation powered by ATP hydrolysis [Danese98].


Subunit of SecD-SecF-YajC-YidC Secretion Complex: inner-membrane protein insertion factor

Synonyms: YidC

Gene: yidC Accession Numbers: EG11197 (EcoCyc), b3705, ECK3698

Locations: inner membrane

Sequence Length: 548 AAs

Molecular Weight: 61.526 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006457 - protein folding Inferred from experiment [Wagner08]
GO:0006461 - protein complex assembly Inferred from experiment [Wagner08]
GO:0051205 - protein insertion into membrane Inferred from experiment Inferred by computational analysis [GOA01, Robinson13, Samuelson00]
GO:0051260 - protein homooligomerization Inferred from experiment [Robinson13]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Klenner08, Scotti00]
GO:0032977 - membrane insertase activity Inferred from experiment [Robinson13, Samuelson00]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, DiazMejia09, Zhang07, Wagner08]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis Inferred from experiment [Saaf98]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Wagner08, Scotti00]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
information transfer protein related chaperoning, repair (refolding)
transport

Unification Links: DIP:DIP-12442N , EcoliWiki:b3705 , Mint:MINT-6477960 , PR:PRO_000023473 , Pride:P25714 , Protein Model Portal:P25714 , RefSeq:NP_418161 , SMR:P25714 , String:511145.b3705 , UniProt:P25714

Relationship Links: InterPro:IN-FAMILY:IPR001708 , InterPro:IN-FAMILY:IPR019998 , InterPro:IN-FAMILY:IPR028053 , InterPro:IN-FAMILY:IPR028055 , Panther:IN-FAMILY:PTHR12428 , PDB:Structure:3BLC , PDB:Structure:3BS6 , Pfam:IN-FAMILY:PF02096 , Pfam:IN-FAMILY:PF14849 , Prints:IN-FAMILY:PR00701 , Prints:IN-FAMILY:PR01900

Summary:
YidC mediates membrane insertion/assembly of inner membrane proteins [Scotti00, Houben00, Samuelson00, Urbanus01, Houben02, vanderLaan03, Yi03]. YidC has been found to interact with the accessory SecDF and YajC proteins of the Sec translocon [Nouwen02] to form a heterotetrameric complex which then, through SecF and YajC interaction with SecY [Sagara94], is believed to facilitate Sec-dependent protein insertion. In addition to its Sec associated function YidC can also insert some membrane proteins such as phage proteins, MtlA, MscL and the F0c subunit of ATP synthase, independently [Samuelson00, Chen02h, vanderLaan04, Facey07, Welte12]. Purified, reconstituted YidC mediates the post-translational insertion of F0c. YidC is required for F0c to adopt its correct oligomerisation state [Robinson13].

YidC is essential [Samuelson00]. YidC depletion causes induction of the Psp stress response [vanderLaan03, Jones03b] resulting from defects in respiratory chain complex biogenesis [vanderLaan03]. YidC has also been implicated in membrane biogenesis of integral membrane subunits of the anaerobic respiratory chain [Price08].

YidC contains 5 transmembrane regions that are connected via a long periplasmic loop to an additional sixth N-terminal transmembrane region [Saaf98, Ravaud08]. A systematic mutational study indicates that the five most C-terminal transmembrane spanning regions are important for YidC activity [Jiang03]. A site-specific cross-linking approach has identified residues within the third transmembrane segement (TM3) which appear to be a generic docking site for hydrophobic domains in growing nascent inner-membrane proteins (IMPs) and provides a protected environment that facilitates their lipid partitioning and folding [Yu08e].

Microscopy of 2D crystals suggests that full-length membrane bound YidC is dimeric [Lotz08]. A 3D structure of YidC in complex with translating ribosome shows dimers of YidC bound at the tunnel exit of the ribosome nascent chain complex [Kohler09]. Momomeric YidC represents the functional unit in vitro [Kedrov13]. Protein purification and cross-linking studies indicate that YidC is physically and functionally connected to FtsH and that this complex may be involved in quality control of inner membrane proteins (IMPs) during biogenesis [vanBloois08]. The C-terminus of YidC is in contact with the ribosome, the signal recognition particle (SRP) and FtsY [Welte12]. E. coli ribosomes do not associate with YidC unless they are synthesizing YidC substrates [Kedrov13].

Defects of an E. coli yidC mutant are functionally complemented by production of chloroplast Alb3 [Jiang02].

YidC localizes to the inner membrane, particularly at the cell poles [Urbanus02]. YidC membrane insertion has been described [Koch02, Urbanus02].

Reviews: [Luirink01, Stuart02, Chen02i, Kuhn03, deGier03, vanderLaan05, Dalbey04, Kiefer07, Kol08a].
Comments: [Stuart00, Herrmann13]

Citations: [vanderLaan01, Samuelson01, Beck01, vanDalen02, Watkins02, Froderberg03, Facey03, Chen03e, Hatzixanthis03, Raine03, Van04b, Martinez08, Klenner08, Sachelaru13, Zhu12b, Kol09, Xie06a, Kol08, vanBloois05, Yuan07, Klenner12, Winterfeld13, Imhof11, Wagner08]

Essentiality data for yidC knockouts: ?

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

Subunit of SecD-SecF-YajC-YidC Secretion Complex: YajC

Gene: yajC Accession Numbers: EG11096 (EcoCyc), b0407, ECK0401

Locations: inner membrane

Sequence Length: 110 AAs

Molecular Weight: 11.887 kD (from nucleotide sequence)

GO Terms:

Cellular Component: GO:0005887 - integral component of plasma membrane Inferred from experiment [Fang11]
GO:0031522 - cell envelope Sec protein transport complex Inferred from experiment [Duong97a]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

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-29531N , EcoliWiki:b0407 , Pride:P0ADZ7 , Protein Model Portal:P0ADZ7 , RefSeq:NP_414941 , SMR:P0ADZ7 , String:511145.b0407 , UniProt:P0ADZ7

Relationship Links: InterPro:IN-FAMILY:IPR003849 , PDB:Structure:2RDD , Pfam:IN-FAMILY:PF02699 , Prints:IN-FAMILY:PR01853

Summary:
YajC is a member of the SecD/SecF/YajC/YidC complex, which functions in concert with SecYEG to stabilize the insertion of SecA and its bound preprotein into the inner membrane. Under conditions of over production YajC forms a complex with both SecYEG and SecDF [Nouwen02]. YajC is not essential for cell viability or protein export [Taura94, Pogliano94a]. Membrane topology experiments indicate that the C-terminus of YajC is located in the cytoplasm and the N-terminus is buried in the membrane [Fang11]. When purifed and expressed the C-terminal portion of YajC exists as a trimer and forms a structure rich in β-strands [Fang11].

Citations: [Duong97a, Duong97, Scotti00, Muller01, Nouwen01, Kato03]

Essentiality data for yajC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of SecD-SecF-YajC-YidC Secretion Complex: SecF

Gene: secF Accession Numbers: EG10940 (EcoCyc), b0409, ECK0403

Locations: inner membrane

Sequence Length: 323 AAs

Molecular Weight: 35.382 kD (from nucleotide sequence)

GO Terms:

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

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: EcoliWiki:b0409 , ModBase:P0AG93 , PR:PRO_000023927 , Pride:P0AG93 , Protein Model Portal:P0AG93 , RefSeq:NP_414943 , SMR:P0AG93 , String:511145.b0409 , UniProt:P0AG93

Relationship Links: InterPro:IN-FAMILY:IPR005665 , InterPro:IN-FAMILY:IPR022645 , InterPro:IN-FAMILY:IPR022646 , InterPro:IN-FAMILY:IPR022813 , Pfam:IN-FAMILY:PF02355 , Pfam:IN-FAMILY:PF07549 , Prints:IN-FAMILY:PR01755

Essentiality data for secF knockouts: ?

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

Subunit of SecD-SecF-YajC-YidC Secretion Complex: SecD

Gene: secD Accession Numbers: EG10938 (EcoCyc), b0408, ECK0402

Locations: inner membrane

Sequence Length: 615 AAs

Molecular Weight: 66.632 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0015031 - protein transport Inferred from experiment Inferred by computational analysis [UniProtGOA11, Gardel87]
GO:0006605 - protein targeting Inferred by computational analysis [GOA06]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006886 - intracellular protein transport Inferred by computational analysis [GOA01]
GO:0043952 - protein transport by the Sec complex Inferred by computational analysis [GOA06]
GO:0065002 - intracellular protein transmembrane transport Inferred by computational analysis [GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0015450 - P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, DiazMejia09, Zhang07, Daley05]
GO:0005622 - intracellular Inferred by computational analysis [GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

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-35837N , EcoliWiki:b0408 , Mint:MINT-1309074 , ModBase:P0AG90 , PR:PRO_000023925 , Pride:P0AG90 , Protein Model Portal:P0AG90 , RefSeq:NP_414942 , SMR:P0AG90 , String:511145.b0408 , UniProt:P0AG90

Relationship Links: InterPro:IN-FAMILY:IPR005791 , InterPro:IN-FAMILY:IPR022645 , InterPro:IN-FAMILY:IPR022646 , InterPro:IN-FAMILY:IPR022813 , InterPro:IN-FAMILY:IPR027398 , Pfam:IN-FAMILY:PF02355 , Pfam:IN-FAMILY:PF07549 , Pfam:IN-FAMILY:PF13721

Summary:
SecD is a membrane component of the SecD/SecF/YajC/YidC complex, which is itself a subclass of the Sec protein secretion complex. Deletions of secD result in cold-sensitive mutants which could be complemented by plasmids expressing the gene [Gardel87]. SecD/SecF/YajC/YidC are believed to stabilize the SecYEG complex, facilitating the insertion of SecA and its bound preprotein into the inner membrane.

Essentiality data for secD knockouts: ?

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

Subunit of Sec Holo-Translocon: SecYEG translocase

Locations: inner membrane

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]

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

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 [Park11a]. 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: [Tam05a, Osborne93, Derman93, Nouwen96, Collinson01]


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 4]
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

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 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

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 [Wang04d].

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 1]

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

Baba90: Baba T, Jacq A, Brickman E, Beckwith J, Taura T, Ueguchi C, Akiyama Y, Ito K (1990). "Characterization of cold-sensitive secY mutants of Escherichia coli." J Bacteriol 172(12);7005-10. PMID: 2254269

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

Beck01: Beck K, Eisner G, Trescher D, Dalbey RE, Brunner J, Muller M (2001). "YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids." EMBO Rep 2(8);709-14. PMID: 11463745

Boy09: Boy D, Koch HG (2009). "Visualization of Distinct Entities of the SecYEG Translocon during Translocation and Integration of Bacterial Proteins." Mol Biol Cell. PMID: 19158385

Breyton02: Breyton C, Haase W, Rapoport TA, Kuhlbrandt W, Collinson I (2002). "Three-dimensional structure of the bacterial protein-translocation complex SecYEG." Nature 418(6898);662-5. PMID: 12167867

Brundage90: Brundage L, Hendrick JP, Schiebel E, Driessen AJ, Wickner W (1990). "The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation." Cell 62(4);649-57. PMID: 2167176

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chen02h: Chen M, Samuelson JC, Jiang F, Muller M, Kuhn A, Dalbey RE (2002). "Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion." J Biol Chem 277(10);7670-5. PMID: 11751917

Chen02i: Chen M, Xie K, Jiang F, Yi L, Dalbey RE (2002). "YidC, a newly defined evolutionarily conserved protein, mediates membrane protein assembly in bacteria." Biol Chem 383(10);1565-72. PMID: 12452432

Chen03e: Chen M, Xie K, Nouwen N, Driessen AJ, Dalbey RE (2003). "Conditional lethal mutations separate the M13 procoat and Pf3 coat functions of YidC: different YIDC structural requirements for membrane protein insertion." J Biol Chem 278(26);23295-300. PMID: 12707259

Collinson01: Collinson I, Breyton C, Duong F, Tziatzios C, Schubert D, Or E, Rapoport T, Kuhlbrandt W (2001). "Projection structure and oligomeric properties of a bacterial core protein translocase." EMBO J 20(10);2462-71. PMID: 11350935

Collinson05: Collinson I (2005). "The structure of the bacterial protein translocation complex SecYEG." Biochem Soc Trans 33(Pt 6);1225-30. PMID: 16246086

Dalal11: Dalal K, Duong F (2011). "The SecY complex: conducting the orchestra of protein translocation." Trends Cell Biol 21(9);506-14. PMID: 21632250

Dalal12: Dalal K, Chan CS, Sligar SG, Duong F (2012). "Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase." Proc Natl Acad Sci U S A 109(11);4104-9. PMID: 22378651

Dalbey04: Dalbey RE, Kuhn A (2004). "YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins." J Cell Biol 166(6);769-74. PMID: 15364957

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

Danese98: Danese PN, Silhavy TJ (1998). "Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli." Annu Rev Genet 32;59-94. PMID: 9928475

deGier03: de Gier JW, Luirink J (2003). "The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins." EMBO Rep 4(10);939-43. PMID: 14528263

deKeyzer03: de Keyzer J, van der Does C, Driessen AJ (2003). "The bacterial translocase: a dynamic protein channel complex." Cell Mol Life Sci 60(10);2034-52. PMID: 14618254

Derman93: Derman AI, Puziss JW, Bassford PJ, Beckwith J (1993). "A signal sequence is not required for protein export in prlA mutants of Escherichia coli." EMBO J 12(3);879-88. PMID: 8458344

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Douville95: Douville K, Price A, Eichler J, Economou A, Wickner W (1995). "SecYEG and SecA are the stoichiometric components of preprotein translocase." J Biol Chem 270(34);20106-11. PMID: 7650029

Driessen08: Driessen AJ, Nouwen N (2008). "Protein translocation across the bacterial cytoplasmic membrane." Annu Rev Biochem 77;643-67. PMID: 18078384

Driessen98: Driessen AJ, Fekkes P, van der Wolk JP (1998). "The Sec system." Curr Opin Microbiol 1(2);216-22. PMID: 10066476

Duong14: Duong F (2014). "Capturing the bacterial holo-complex." Proc Natl Acad Sci U S A 111(13);4739-40. PMID: 24707040

Duong97: Duong F, Wickner W (1997). "The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling." EMBO J 16(16);4871-9. PMID: 9305629

Duong97a: Duong F, Wickner W (1997). "Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme." EMBO J 16(10);2756-68. PMID: 9184221

duPlessis11: du Plessis DJ, Nouwen N, Driessen AJ (2011). "The Sec translocase." Biochim Biophys Acta 1808(3);851-65. PMID: 20801097

Facey03: Facey SJ, Kuhn A (2003). "The sensor protein KdpD inserts into the Escherichia coli membrane independent of the Sec translocase and YidC." Eur J Biochem 270(8);1724-34. PMID: 12694185

Facey07: Facey SJ, Neugebauer SA, Krauss S, Kuhn A (2007). "The mechanosensitive channel protein MscL is targeted by the SRP to the novel YidC membrane insertion pathway of Escherichia coli." J Mol Biol 365(4);995-1004. PMID: 17113597

Fang11: Fang J, Wei Y (2011). "Expression, purification and characterization of the Escherichia coli integral membrane protein YajC." Protein Pept Lett 18(6);601-8. PMID: 21235483

Flower01: Flower AM (2001). "SecG function and phospholipid metabolism in Escherichia coli." J Bacteriol 183(6);2006-12. PMID: 11222599

Frauenfeld11: Frauenfeld J, Gumbart J, Sluis EO, Funes S, Gartmann M, Beatrix B, Mielke T, Berninghausen O, Becker T, Schulten K, Beckmann R (2011). "Cryo-EM structure of the ribosome-SecYE complex in the membrane environment." Nat Struct Mol Biol 18(5);614-21. PMID: 21499241

Froderberg03: Froderberg L, Houben E, Samuelson JC, Chen M, Park SK, Phillips GJ, Dalbey R, Luirink J, De Gier JW (2003). "Versatility of inner membrane protein biogenesis in Escherichia coli." Mol Microbiol 47(4);1015-27. PMID: 12581356

Gardel87: Gardel C, Benson S, Hunt J, Michaelis S, Beckwith J (1987). "secD, a new gene involved in protein export in Escherichia coli." J Bacteriol 169(3);1286-90. PMID: 3029032

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gold07: Gold VA, Duong F, Collinson I (2007). "Structure and function of the bacterial Sec translocon." Mol Membr Biol 24(5-6);387-94. PMID: 17710643

Hanada96: Hanada M, Nishiyama K, Tokuda H (1996). "SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature." FEBS Lett 381(1-2);25-8. PMID: 8641431

Hatzixanthis03: Hatzixanthis K, Palmer T, Sargent F (2003). "A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase." Mol Microbiol 49(5);1377-90. PMID: 12940994

Herrmann13: Herrmann JM (2013). "The bacterial membrane insertase YidC is a functional monomer and binds ribosomes in a nascent chain-dependent manner." J Mol Biol 425(22);4071-3. PMID: 23933056

Hizlan12: Hizlan D, Robson A, Whitehouse S, Gold VA, Vonck J, Mills D, Kuhlbrandt W, Collinson I (2012). "Structure of the SecY complex unlocked by a preprotein mimic." Cell Rep 1(1);21-8. PMID: 22576621

Homma97: Homma T, Yoshihisa T, Ito K (1997). "Subunit interactions in the Escherichia coli protein translocase: SecE and SecG associate independently with SecY." FEBS Lett 408(1);11-5. PMID: 9180258

Houben00: Houben EN, Scotti PA, Valent QA, Brunner J, de Gier JL, Oudega B, Luirink J (2000). "Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA." FEBS Lett 476(3);229-33. PMID: 10913619

Houben02: Houben EN, Urbanus ML, Van Der Laan M, Ten Hagen-Jongman CM, Driessen AJ, Brunner J, Oudega B, Luirink J (2002). "YidC and SecY mediate membrane insertion of a Type I transmembrane domain." J Biol Chem 277(39);35880-6. PMID: 12107184

Imhof11: Imhof N, Kuhn A, Gerken U (2011). "Substrate-dependent conformational dynamics of the Escherichia coli membrane insertase YidC." Biochemistry 50(15);3229-39. PMID: 21401071

Ito83: Ito K, Wittekind M, Nomura M, Shiba K, Yura T, Miura A, Nashimoto H (1983). "A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins." Cell 32(3);789-97. PMID: 6339072

Ito84: Ito K, Cerretti DP, Nashimoto H, Nomura M (1984). "Characterization of an amber mutation in the structural gene for ribosomal protein L15, which impairs the expression of the protein export gene, secY, in Escherichia coli." EMBO J 3(10);2319-24. PMID: 6389119

Ito90a: Ito K (1990). "Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export." J Bioenerg Biomembr 22(3);353-67. PMID: 2202723

Jiang02: Jiang F, Yi L, Moore M, Chen M, Rohl T, Van Wijk KJ, De Gier JW, Henry R, Dalbey RE (2002). "Chloroplast YidC homolog Albino3 can functionally complement the bacterial YidC depletion strain and promote membrane insertion of both bacterial and chloroplast thylakoid proteins." J Biol Chem 277(22);19281-8. PMID: 11891220

Jiang03: Jiang F, Chen M, Yi L, De Gier JW, Kuhn A, Dalbey RE (2003). "Defining the regions of the Escherichia coli YidC that contribute to activity." J Biol Chem 278(49):48965-72. PMID: 14506280

Joly93: Joly JC, Wickner W (1993). "The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids." EMBO J 12(1);255-63. PMID: 8428583

Jones03b: Jones SE, Lloyd LJ, Tan KK, Buck M (2003). "Secretion defects that activate the phage shock response of Escherichia coli." J Bacteriol 185(22);6707-11. PMID: 14594846

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Karamanou08: Karamanou S, Bariami V, Papanikou E, Kalodimos CG, Economou A (2008). "Assembly of the translocase motor onto the preprotein-conducting channel." Mol Microbiol 70(2);311-22. PMID: 18761620

Kato03: Kato Y, Nishiyama K, Tokuda H (2003). "Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction." FEBS Lett 550(1-3);114-8. PMID: 12935896

Kedrov11: Kedrov A, Kusters I, Krasnikov VV, Driessen AJ (2011). "A single copy of SecYEG is sufficient for preprotein translocation." EMBO J 30(21);4387-97. PMID: 21897368

Kedrov13: Kedrov A, Sustarsic M, de Keyzer J, Caumanns JJ, Wu ZC, Driessen AJ (2013). "Elucidating the native architecture of the YidC: ribosome complex." J Mol Biol 425(22);4112-24. PMID: 23933010

Kiefer07: Kiefer D, Kuhn A (2007). "YidC as an essential and multifunctional component in membrane protein assembly." Int Rev Cytol 259;113-38. PMID: 17425940

Klenner08: Klenner C, Yuan J, Dalbey RE, Kuhn A (2008). "The Pf3 coat protein contacts TM1 and TM3 of YidC during membrane biogenesis." FEBS Lett 582(29);3967-72. PMID: 18996118

Klenner12: Klenner C, Kuhn A (2012). "Dynamic disulfide scanning of the membrane-inserting Pf3 coat protein reveals multiple YidC substrate contacts." J Biol Chem 287(6);3769-76. PMID: 22179606

Koch02: Koch HG, Moser M, Schimz KL, Muller M (2002). "The integration of YidC into the cytoplasmic membrane of Escherichia coli requires the signal recognition particle, SecA and SecYEG." J Biol Chem 277(8);5715-8. PMID: 11777926

Kohler09: Kohler R, Boehringer D, Greber B, Bingel-Erlenmeyer R, Collinson I, Schaffitzel C, Ban N (2009). "YidC and Oxa1 form dimeric insertion pores on the translating ribosome." Mol Cell 34(3);344-53. PMID: 19450532

Kol08: Kol S, Nouwen N, Driessen AJ (2008). "The charge distribution in the cytoplasmic loop of subunit C of the F1F0 ATPase is a determinant for YidC targeting." J Biol Chem 283(15);9871-7. PMID: 18276587

Kol08a: Kol S, Nouwen N, Driessen AJ (2008). "Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes." J Biol Chem 283(46);31269-73. PMID: 18658156

Kol09: Kol S, Majczak W, Heerlien R, van der Berg JP, Nouwen N, Driessen AJ (2009). "Subunit a of the F(1)F(0) ATP synthase requires YidC and SecYEG for membrane insertion." J Mol Biol 390(5);893-901. PMID: 19497329

Kuhn03: Kuhn A, Stuart R, Henry R, Dalbey RE (2003). "The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion?." Trends Cell Biol 13(10);510-6. PMID: 14507478

Lotz08: Lotz M, Haase W, Kuhlbrandt W, Collinson I (2008). "Projection structure of yidC: a conserved mediator of membrane protein assembly." J Mol Biol 375(4);901-7. PMID: 18054957

Luirink01: Luirink J, Samuelsson T, de Gier JW (2001). "YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly." FEBS Lett 501(1);1-5. PMID: 11457446

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

Martinez08: Martinez Molina D, Lundback AK, Niegowski D, Eshaghi S (2008). "Expression and purification of the recombinant membrane protein YidC: A case study for increased stability and solubility." Protein Expr Purif 62(1):49-52. PMID: 18586516

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

Muller01: Muller M, Koch HG, Beck K, Schafer U (2001). "Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane." Prog Nucleic Acid Res Mol Biol 66;107-57. PMID: 11051763

Nouwen01: Nouwen N, van der Laan M, Driessen AJ (2001). "SecDFyajC is not required for the maintenance of the proton motive force." FEBS Lett 508(1);103-6. PMID: 11707277

Nouwen02: Nouwen N, Driessen AJ (2002). "SecDFyajC forms a heterotetrameric complex with YidC." Mol Microbiol 44(5);1397-405. PMID: 12068816

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

Park11a: Park E, Rapoport TA (2011). "Preserving the membrane barrier for small molecules during bacterial protein translocation." Nature 473(7346);239-42. PMID: 21562565

Park13: Park E, Menetret JF, Gumbart JC, Ludtke SJ, Li W, Whynot A, Rapoport TA, Akey CW (2013). "Structure of the SecY channel during initiation of protein translocation." Nature. PMID: 24153188

Pogliano94: Pogliano JA, Beckwith J (1994). "SecD and SecF facilitate protein export in Escherichia coli." EMBO J 13(3);554-61. PMID: 8313900

Pogliano94a: Pogliano KJ, Beckwith J (1994). "Genetic and molecular characterization of the Escherichia coli secD operon and its products." J Bacteriol 176(3);804-14. PMID: 7507921

Price08: Price CE, Driessen AJ (2008). "YidC is involved in the biogenesis of anaerobic respiratory complexes in the inner membrane of Escherichia coli." J Biol Chem 283(40):26921-7. PMID: 18635537

Raine03: Raine A, Ullers R, Pavlov M, Luirink J, Wikberg JE, Ehrenberg M (2003). "Targeting and insertion of heterologous membrane proteins in E. coli." Biochimie 85(7);659-68. PMID: 14505821

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Ravaud08: Ravaud S, Stjepanovic G, Wild K, Sinning I (2008). "The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft." J Biol Chem 283(14);9350-8. PMID: 18234665

Riggs88: Riggs PD, Derman AI, Beckwith J (1988). "A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene." Genetics 118(4);571-9. PMID: 3284784

Robinson13: Robinson PJ, Woolhead CA (2013). "Post-translational membrane insertion of an endogenous YidC substrate." Biochim Biophys Acta 1833(12);2781-8. PMID: 23872420

Robson09: Robson A, Carr B, Sessions RB, Collinson I (2009). "Synthetic peptides identify a second periplasmic site for the plug of the SecYEG protein translocation complex." FEBS Lett 583(1);207-12. PMID: 19084013

Rusch07: Rusch SL, Kendall DA (2007). "Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon." Biochim Biophys Acta 1768(1);5-12. PMID: 17011510

Saaf98: Saaf A, Monne M, de Gier JW, von Heijne G (1998). "Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli." J Biol Chem 273(46);30415-8. PMID: 9804807

Sachelaru13: Sachelaru I, Petriman NA, Kudva R, Kuhn P, Welte T, Knapp B, Drepper F, Warscheid B, Koch HG (2013). "YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein." J Biol Chem 288(23);16295-307. PMID: 23609445

Sagara94: Sagara K, Matsuyama S, Mizushima S (1994). "SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane." J Bacteriol 176(13);4111-6. PMID: 8021192

Samuelson00: Samuelson JC, Chen M, Jiang F, Moller I, Wiedmann M, Kuhn A, Phillips GJ, Dalbey RE (2000). "YidC mediates membrane protein insertion in bacteria." Nature 406(6796);637-41. PMID: 10949305

Samuelson01: Samuelson JC, Jiang F, Yi L, Chen M, de Gier JW, Kuhn A, Dalbey RE (2001). "Function of YidC for the insertion of M13 procoat protein in Escherichia coli: translocation of mutants that show differences in their membrane potential dependence and Sec requirement." J Biol Chem 276(37);34847-52. PMID: 11457858

Satoh03: Satoh Y, Matsumoto G, Mori H, Ito K (2003). "Nearest neighbor analysis of the SecYEG complex. 1. Identification of a SecY-SecG interface." Biochemistry 42(24);7434-41. PMID: 12809499

Satoh03a: Satoh Y, Mori H, Ito K (2003). "Nearest neighbor analysis of the SecYEG complex. 2. Identification of a SecY-SecE cytosolic interface." Biochemistry 42(24);7442-7. PMID: 12809500

Schatz89: Schatz PJ, Riggs PD, Jacq A, Fath MJ, Beckwith J (1989). "The secE gene encodes an integral membrane protein required for protein export in Escherichia coli." Genes Dev 3(7);1035-44. PMID: 2673920

Scheuring05: Scheuring J, Braun N, Nothdurft L, Stumpf M, Veenendaal AK, Kol S, van der Does C, Driessen AJ, Weinkauf S (2005). "The oligomeric distribution of SecYEG is altered by SecA and translocation ligands." J Mol Biol 354(2);258-71. PMID: 16242710

Schulze14: Schulze RJ, Komar J, Botte M, Allen WJ, Whitehouse S, Gold VA, Lycklama A Nijeholt JA, Huard K, Berger I, Schaffitzel C, Collinson I (2014). "Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC." Proc Natl Acad Sci U S A 111(13);4844-9. PMID: 24550475

Scotti00: Scotti PA, Urbanus ML, Brunner J, de Gier JW, von Heijne G, van der Does C, Driessen AJ, Oudega B, Luirink J (2000). "YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase." EMBO J 19(4);542-9. PMID: 10675323

Shiba84: Shiba K, Ito K, Yura T, Cerretti DP (1984). "A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant." EMBO J 3(3);631-5. PMID: 6370688

Shimokawa03: Shimokawa N, Mori H, Ito K (2003). "Importance of transmembrane segments in Escherichia coli SecY." Mol Genet Genomics 269(2);180-7. PMID: 12756530

Snyders97: Snyders S, Ramamurthy V, Oliver D (1997). "Identification of a region of interaction between Escherichia coli SecA and SecY proteins." J Biol Chem 272(17);11302-6. PMID: 9111035

Stuart00: Stuart RA, Neupert W (2000). "Making membranes in bacteria." Nature 406(6796);575, 577. PMID: 10949283

Stuart02: Stuart R (2002). "Insertion of proteins into the inner membrane of mitochondria: the role of the Oxa1 complex." Biochim Biophys Acta 1592(1);79-87. PMID: 12191770

Tam05a: Tam PC, Maillard AP, Chan KK, Duong F (2005). "Investigating the SecY plug movement at the SecYEG translocation channel." EMBO J 24(19);3380-8. PMID: 16148946

Taufik13: Taufik I, Kedrov A, Exterkate M, Driessen AJ (2013). "Monitoring the activity of single translocons." J Mol Biol 425(22);4145-53. PMID: 23968858

Taura94: Taura T, Akiyama Y, Ito K (1994). "Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes." Mol Gen Genet 243(3);261-9. PMID: 8190079

Tziatzios04: Tziatzios C, Schubert D, Lotz M, Gundogan D, Betz H, Schagger H, Haase W, Duong F, Collinson I (2004). "The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules." J Mol Biol 340(3);513-24. PMID: 15210351

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Urbanus01: Urbanus ML, Scotti PA, Froderberg L, Saaf A, de Gier JW, Brunner J, Samuelson JC, Dalbey RE, Oudega B, Luirink J (2001). "Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC." EMBO Rep 2(6);524-9. PMID: 11415986

Urbanus02: Urbanus ML, Froderberg L, Drew D, Bjork P, de Gier JW, Brunner J, Oudega B, Luirink J (2002). "Targeting, insertion, and localization of Escherichia coli YidC." J Biol Chem 277(15);12718-23. PMID: 11821429

Van04b: Van Der Laan M, Nouwen N, Driessen AJ (2004). "SecYEG proteoliposomes catalyze the delta psi-dependent membrane insertion of FtsQ." J Biol Chem 279(3):1659-64. PMID: 14578344

Van04c: Van den Berg B, Clemons WM, Collinson I, Modis Y, Hartmann E, Harrison SC, Rapoport TA (2004). "X-ray structure of a protein-conducting channel." Nature 427(6969);36-44. PMID: 14661030

vanBloois05: van Bloois E, Nagamori S, Koningstein G, Ullers RS, Preuss M, Oudega B, Harms N, Kaback HR, Herrmann JM, Luirink J (2005). "The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential." J Biol Chem 280(13);12996-3003. PMID: 15671040

vanBloois08: van Bloois E, Dekker HL, Froderberg L, Houben EN, Urbanus ML, de Koster CG, de Gier JW, Luirink J (2008). "Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins." FEBS Lett 582(10);1419-24. PMID: 18387365

vanDalen02: van Dalen A, van der Laan M, Driessen AJ, Killian JA, de Kruijff B (2002). "Components required for membrane assembly of newly synthesized K+ channel KcsA." FEBS Lett 511(1-3);51-8. PMID: 11821048

vanderLaan01: van der Laan M, Houben EN, Nouwen N, Luirink J, Driessen AJ (2001). "Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner." EMBO Rep 2(6);519-23. PMID: 11415985

vanderLaan03: van der Laan M, Urbanus ML, Ten Hagen-Jongman CM, Nouwen N, Oudega B, Harms N, Driessen AJ, Luirink J (2003). "A conserved function of YidC in the biogenesis of respiratory chain complexes." Proc Natl Acad Sci U S A 100(10);5801-6. PMID: 12724529

vanderLaan04: van der Laan M, Bechtluft P, Kol S, Nouwen N, Driessen AJ (2004). "F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis." J Cell Biol 165(2);213-22. PMID: 15096523

vanderLaan05: van der Laan M, Nouwen NP, Driessen AJ (2005). "YidC--an evolutionary conserved device for the assembly of energy-transducing membrane protein complexes." Curr Opin Microbiol 8(2);182-7. PMID: 15802250

vanderSluis02: van der Sluis EO, Nouwen N, Driessen AJ (2002). "SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking." FEBS Lett 527(1-3);159-65. PMID: 12220653

Veenendaal01: Veenendaal AK, van der Does C, Driessen AJ (2001). "Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis." J Biol Chem 276(35);32559-66. PMID: 11445571

Wagner08: Wagner S, Pop OI, Pop O, Haan GJ, Baars L, Koningstein G, Klepsch MM, Genevaux P, Luirink J, de Gier JW (2008). "Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC." J Biol Chem 283(26);17881-90. PMID: 18456666

Wang04d: Wang L, Miller A, Rusch SL, Kendall DA (2004). "Demonstration of a specific Escherichia coli SecY-signal peptide interaction." Biochemistry 43(41);13185-92. PMID: 15476412

Watanabe89b: Watanabe M, Blobel G (1989). "Site-specific antibodies against the PrlA (secY) protein of Escherichia coli inhibit protein export by interfering with plasma membrane binding of preproteins." Proc Natl Acad Sci U S A 86(6);1895-9. PMID: 2538820

Watkins02: Watkins WE, Menon AK (2002). "Reconstitution of phospholipid flippase activity from E. coli inner membrane: a test of the protein translocon as a candidate flippase." Biol Chem 383(9);1435-40. PMID: 12437136

Welte12: Welte T, Kudva R, Kuhn P, Sturm L, Braig D, Muller M, Warscheid B, Drepper F, Koch HG (2012). "Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle." Mol Biol Cell 23(3);464-79. PMID: 22160593

Winterfeld13: Winterfeld S, Ernst S, Borsch M, Gerken U, Kuhn A (2013). "Real time observation of single membrane protein insertion events by the Escherichia coli insertase YidC." PLoS One 8(3);e59023. PMID: 23527078

Xie06a: Xie K, Kiefer D, Nagler G, Dalbey RE, Kuhn A (2006). "Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity." Biochemistry 45(44);13401-8. PMID: 17073462

Yi03: Yi L, Jiang F, Chen M, Cain B, Bolhuis A, Dalbey RE (2003). "YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase." Biochemistry 42(35);10537-44. PMID: 12950181

Yu08e: Yu Z, Koningstein G, Pop A, Luirink J (2008). "The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins." J Biol Chem 283(50):34635-42. PMID: 18840604

Yuan07: Yuan J, Phillips GJ, Dalbey RE (2007). "Isolation of cold-sensitive yidC mutants provides insights into the substrate profile of the YidC insertase and the importance of transmembrane 3 in YidC function." J Bacteriol 189(24);8961-72. PMID: 17933892

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zhu12b: Zhu L, Klenner C, Kuhn A, Dalbey RE (2012). "Both YidC and SecYEG are required for translocation of the periplasmic loops 1 and 2 of the multispanning membrane protein TatC." J Mol Biol 424(5);354-67. PMID: 23058713


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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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