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Escherichia coli K-12 substr. MG1655 Polypeptide: inner-membrane protein insertion factor
Inferred from experiment

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

Regulation Summary Diagram

Regulation summary diagram for yidC

Component of:
SecD-SecF-YajC-YidC Secretion Complex (extended summary available)
Sec Holo-Translocon (extended summary available)

YidC mediates membrane insertion/assembly of inner membrane proteins [Scotti00, Houben00, Samuelson00, Urbanus01, Houben02, vanderLaan03, Yi03a]. 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, Chen02c, 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, Jones03a] 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 [Yu08a].

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, Chen02d, Kuhn03, deGier03, vanderLaan05, Dalbey04, Kiefer07, Kol08a].
Comments: [Stuart00, Herrmann13]

Citations: [vanderLaan01, Samuelson01, Beck01, vanDalen02, Watkins02, Froderberg03, Facey03, Chen03d , Hatzixanthis03, Raine03, Van04b, Martinez08, Klenner08, Sachelaru13, Zhu12a, Kol09, Xie06 , Kol08, vanBloois05, Yuan07, Klenner12, Winterfeld13, Imhof11, Wagner08 ]

Locations: inner membrane

Map Position: [3,883,099 -> 3,884,745] (83.69 centisomes, 301°)
Length: 1647 bp / 548 aa

Molecular Weight of Polypeptide: 61.526 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0012120, DIP:DIP-12442N, EchoBASE:EB1183, EcoGene:EG11197, EcoliWiki:b3705, Mint:MINT-6477960, OU-Microarray:b3705, PortEco:yidC, PR:PRO_000023473, Pride:P25714, Protein Model Portal:P25714, RefSeq:NP_418161, RegulonDB:EG11197, 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, PDB:Structure:4UTQ, Pfam:IN-FAMILY:PF02096, Pfam:IN-FAMILY:PF14849, Prints:IN-FAMILY:PR00701, Prints:IN-FAMILY:PR01900

Gene-Reaction Schematic

Gene-Reaction Schematic

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

MultiFun Terms: cell structuremembrane
information transferprotein relatedchaperoning, repair (refolding)

Essentiality data for yidC knockouts:

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

Last-Curated 22-Jan-2014 by Mackie A, Macquarie University

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

Subunit composition of SecD-SecF-YajC-YidC Secretion Complex = [YidC][YajC][SecF][SecD]
         inner-membrane protein insertion factor = YidC (extended summary available)

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

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 [Duong97a]. 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 [Danese98a].

Subunit of: Sec Holo-Translocon

Inferred from experiment

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)

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

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

Sequence Features

Protein sequence of inner-membrane protein insertion factor with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 6 -> 23
Inferred by curator[UniProt15]
UniProt: Helical.
Mutagenesis-Variant 24 -> 27
Author statement[UniProt15]
UniProt: Cold-sensitive at 30 degrees Celsius; when associated with 334-W--G-338. Protein accumulates stably.
Protein-Segment 24 -> 264
Author statement[UniProt15]
UniProt: Can be removed without causing lethality, dispensible for M13 procoat processing; Sequence Annotation Type: region of interest.
Protein-Segment 215 -> 265
Author statement[UniProt15]
UniProt: Interacts with SecF; not required for insertion of a number of Sec-dependent or Sec-independent substrates; Sequence Annotation Type: region of interest.
Protein-Segment 265 -> 346
Author statement[UniProt15]
UniProt: Required for Sec-dependent and Sec-independent protein insertion; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 334 -> 338
Inferred from experiment[Chen03d]
UniProt: Cold-sensitive at 30 degrees Celsius; when associated with 24-I--R-27. Protein accumulates stably.
Transmembrane-Region 343 -> 370
Inferred by curator[UniProt15]
UniProt: Helical.
Mutagenesis-Variant 361
Inferred from experiment[Jiang03]
UniProt: Loss of function.
Transmembrane-Region 417 -> 446
Inferred by curator[UniProt15]
UniProt: Helical.
Mutagenesis-Variant 436
Inferred from experiment[Jiang03]
UniProt: Loss of function.
Transmembrane-Region 464 -> 481
Inferred by curator[UniProt15]
UniProt: Helical.
Mutagenesis-Variant 483 -> 487
Inferred from experiment[Chen03d]
UniProt: Temperature-sensitive at 42 degrees Celsius; when associated with 512-ENLYFQG. Protein is not stable.
Transmembrane-Region 494 -> 509
Inferred by curator[UniProt15]
UniProt: Helical.
Mutagenesis-Variant 512
Inferred from experiment[Chen03d]
UniProt: Temperature-sensitive at 42 degrees Celsius; when associated with 483-L--S-487. Protein is not stable.
Transmembrane-Region 513 -> 535
Inferred by curator[UniProt15]
UniProt: Helical.
Protein-Segment 527 -> 548
Author statement[UniProt15]
UniProt: Can be removed without causing lethality, dispensible for M13 procoat processing; Sequence Annotation Type: region of interest.

Sequence Pfam Features

Protein sequence of inner-membrane protein insertion factor with features indicated

Feature Class Location Citations Comment
Pfam PF14849 61 -> 343
Inferred by computational analysis[Finn14]
YidC_periplas : YidC periplasmic domain
Pfam PF02096 354 -> 533
Inferred by computational analysis[Finn14]
60KD_IMP : 60Kd inner membrane protein

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

The database does not contain any information about transcription units for this gene.

10/20/97 Gene b3705 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11197; confirmed by SwissProt match.


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

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

Chen02c: 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

Chen02d: 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

Chen03d: 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

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

Danese98a: 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

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

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

Duong97a: 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

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

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

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

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

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

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

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

Jones03a: 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

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

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

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

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

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

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

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

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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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