STEPdb: Sub-cellular Topologies of E.coli Polypeptides.

Table: Protein Export Systems in E.coli K-12 (MG1655)  Export to Excel  

Export System
Complete Name
Secretion System
The essential sec secretory pathway from which most of the proteins are secreted or inserted into the plasma membrane.
PMID: 12475201 Paetzel et al: Signal peptidases. Chem Rev 2002
PMID: 17938627 Papanikou et al: Bacterial protein secretion through the translocase nanomachine. Nat Rev Microbiol 2007
PMID: 23216251 Chatzi et al: Breaking on through to the other side: protein export through the bacterial Sec system. Biochem J 2013
Signal Recognition Particle (SRP) - SEC
Co-translational export pathway, known to mainly target and insert transmembrane proteins into the plasma membrane.
PMID: 11101515 Neumann-Haefelin Cet al : SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein. EMBO J. 2000
PMID: 12475201 Paetzel et al: Signal peptidases. Chem Rev 2002
PMID: 17938627 Papanikou et al: Bacterial protein secretion through the translocase nanomachine. Nat Rev Microbiol 2007
PMID: 23216251 Chatzi et al: Breaking on through to the other side: protein export through the bacterial Sec system. Biochem J 2013
PMID: 23563142 von Loeffelholz O et al: Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex. Nat Struct Mol Biol. 2013
Localization Of Lipoproteins
Lipoprotein sorting system
PMID: 15221203 Narita et al: Lipoprotein trafficking in Escherichia coli. Arch Microbiol 2004
PMID: 17498646 Miyamoto & Tokuda: Diverse effects of phospholipids on lipoprotein sorting and ATP hydrolysis by the ABC transporter LolCDE complex. Biochim Biophys Acta 2007 PMID: 19270402 Tokuda H: Biogenesis of outer membranes in Gram-negative bacteria. Biosci Biotechnol Biochem. 2009 PMID: 21663440 Okuda S and Tokuda H: Lipoprotein sorting in bacteria. Annu Rev Microbiol. 2011
β-Barrel Assembly Machinery
Bam complex for the β-Barrel Membrane protein assembly
PMID: 22221898 Rigel & Silhavy: Making a beta-barrel: assembly of outer membrane proteins in Gram-negative bacteria. Curr Opin Microbiol 2012
PMID: 23240560 Patel GJ: Biogenesis of beta-barrel integral proteins of bacterial outer membrane. Biochemistry Mosc 2012
Translocation and assembly module
Archetypal protein transport system, that promotes efficient secretion of autotransporters in proteobacteria.
PMID: 22466966 Selkrig J et al: Discovery of an archetypal protein transport system in bacterial outer membranes. Nat Struct Mol Biol. 2012 PMID: 18047580 Ieva R et al: Incorporation of a polypeptide segment into the beta-domain pore during the assembly of a bacterial autotransporter. Mol Microbiol. 2008
Chaperone Usher export system
pathway known to assemble and secrete adhesive surface structures, called pili or fimbriae, which play essential roles in targeting bacterial pathogens to the host.
PMID: 19820722 Waksman & Hultgren: Structural biology of the chaperone-usher pathway of pilus biogenesis. Nat Rev Microbiol 2009
PMID: 20004668 Nishiyama & Glockshuber: The outer membrane usher guarantees the formation of functional pili by selectively catalyzing donor-strand exchange between subunits that are adjacent in the mature pilus. J Mol Biol 2010
PMID: 20070257Rego et al: Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis. Biochem J 2010
PMID: 22645361 Volkan et al: Domain activities of PapC usher reveal the mechanism of action of an Escherichia coli molecular machine. Proc Natl Acad Sci U S A 2012
PMID: 22411982 Busch & Waksman: Chaperone-usher pathways: diversity and pilus assembly mechanism. Philos Trans R Soc Lond B Biol Sci 2012
Type VI Secretion System
This includes the secretion pathway of autotransporters which is composed of three functional domains: leader sequence, the passenger domain and the β-domain
PMID: 11201256 Henderson et al: Autotransporter proteins, evolution and redefining protein secretion. Trends Microbiol 2000
Major proteinaceous component of a complex extracellular matrix produced by many Enterobacteriaceae.
PMID: 16704339 Barnhart & Chapman: Curli biogenesis and function. Annu Rev Microbiol 2006, PMID: 19131513 Nenninger, A. A. et al: Localized and efficient curli nucleation requires the chaperone-like amyloid assembly protein CsgF Proc Natl Acad Sci U S A 2009, PMID: 16420357 Robinson LS et al: Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein. Mol Microbiol. 2006
Outer membrane vesicles
Outer membrane vesicles
PMID: 17787032 Lee et al Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli. Proteomics 2007
PMID: 18226201 Maribasappa Karched et al: Vesicle-independent extracellular release of a proinflammatory outer membrane lipoprotein in free-soluble form BMC Microbiol 2008 , PMID: 22658749 Prehna et al: A protein export pathway involving Escherichia coli porins. Structure 2012, PMID: 14532000 Wai SN et al: Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin. Cell, 2003
Type II Secretion System
Type two secretion system which mediates secretion of multimeric proteins that are folded in the periplasm
PMID: 18461043 Forest: The type II secretion arrowhead: the structure of GspI-GspJ-GspK. Nat Struct Mol Biol 2008
PMID: 11118204 Francetic et al: Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion. EMBO J 2000, PMID: 22466878 Korotkov KV: The type II secretion system: biogenesis, molecular architecture and mechanism. Nat Rev Microbiol. 2012,
PMID: 22425326 McLaughlin LS: Structural insights into the Type II secretion nanomachine. 22425326 2012,
PMID: 22411978 Douzi B: On the path to uncover the bacterial type II secretion system. Philos Trans R Soc Lond B Biol Sci.2012
Twin-arginine Translocation Pathway
The twin-arginine translocation (Tat) pathway is a protein transport system for the export of folded proteins. Substrate proteins are targeted to the Tat translocase by N-terminal signal peptides harboring a distinctive R-R-x-Phi-Phi "twin-arginine"
PMID: 18715784 De Buck et al: The importance of the twin-arginine translocation pathway for bacterial virulence. Trends Microbiol 2008, PMID: 17581816 Frielingsdorf S: Prerequisites for terminal processing of thylakoidal Tat substrates. J Biol Chem 2007, PMID: 16756481 Lee PA: The bacterial twin-arginine translocation pathway Annual Review of Microbiology 2006 PMID: 21126506 Robinson C et al: Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. Biochim Biophys Acta. 2011
This is a motion generation organelle able to secrete some of it's constituent proteins
PMID: 12730325 Macnab et al: How bacteria assemble flagella. Annual Review of Microbiology 2003
PMID: 21999994 Van Gerven et al: Pili and flagella biology, structure, and biotechnological applications. Prog Mol Biol Transl Sci 2011
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