E.coli K-12 (MG1655) Exportome

UniProt Name:
Type-1 fimbrial protein, A chain (Type-1A pilin)
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Fim operon (class ??1); Fimbrial Subunit. Experimentally verified signal peptide PMID: 2858471 Disulfide bridge (44 84) Disulfide bond-containing protein PMID: 25664544
References:
PMID: 20345943 PMID: 25664544 PMID: 2858471 PMID: 6147250
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19348461 PMID: 19767571 PMID: 20803007 PMID: 18425732
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
21.4 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Common fold of diphtheria toxin/transcription factors/cytochrome f SCOP: 49379
Super Family:
Bacterial adhesins
SCOP: 49401

Go to Complexes

UniProt Name:
Flagellin
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Flameint protein, flagellin. Flagella proteins contribute to the production of outer membrane vesicles. Analysis of E. coli W3110 OMVs revealed that they contain abundant levels of FliC. Compared to the parental strain expressing wild-type fliC, an E. coli strain with a fliC-null mutation produced reduced amounts of OMVs based on both protein and phosphate levels. Identified in nucleoids collected by sucrose gradient centrifugation and analyzed by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). PMID: 21541338 PMID: 12730325
References:
PMID: 12730325 PMID: 21541338 PMID: 24134841
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 17595003 PMID: 17137328 PMID: 20222674 PMID: 19767571
Proteomics / Inner Membrane fraction:
PMID: 17309111

Protein molec/cell:
-
PaxDb:
1212 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
Phase 1 flagellin SCOP: 64517
Super Family:
Phase 1 flagellin
SCOP: 64518

Go to Complexes

UniProt Name:
Protein FimF
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Fim operon (class ??1); Fimbrial Subunit. Required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae. PMID: 15372038 Disulfide bridge (38 78) Disulfide bond-containing protein PMID: 25664544
References:
PMID: 15372038 PMID: 19820722 PMID: 20345943 PMID: 25664544 PMID: 2890081
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19767571 PMID: 18425732
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Common fold of diphtheria toxin/transcription factors/cytochrome f SCOP: 49379
Super Family:
Bacterial adhesins
SCOP: 49401

Go to Complexes

UniProt Name:
Protein FimG
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Fim operon (class ??1); Fimbrial Subunit. Required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae. PMID: 15372038 Disulfide bridge (39 77) Disulfide bond-containing protein PMID: 25664544
References:
PMID: 15372038 PMID: 19820722 PMID: 20345943 PMID: 25664544 PMID: 2890081
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
-
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Common fold of diphtheria toxin/transcription factors/cytochrome f SCOP: 49379
Super Family:
Bacterial adhesins
SCOP: 49401

Go to Complexes

UniProt Name:
Type 1 fimbrin D-mannose specific adhesin (Protein FimH)
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Fim operon (class ??1); Potential tip-adhesin. Required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae. PMID: 1971261 PMID: 2900235 PMID: 2890081
References:
PMID: 1971261 PMID: 19820722 PMID: 20345943 PMID: 24140205 PMID: 2890081 PMID: 2900235
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19767571
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Common fold of diphtheria toxin/transcription factors/cytochrome f SCOP: 49379
Super Family:
Bacterial adhesins
SCOP: 49401

Go to Complexes

UniProt Name:
Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
Localization:
Cytoplasmic, Peripheral inner membrane protein facing the cytoplasm, Peripheral outer membrane protein facing the extra-cellular space
Notes:
When modified at Lys342 possibly secreted by an unknown mechanism, no evidence of signal peptide) Homodimer, stabilized by Mg2+; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. Essential for the degradation of carbohydrates via glycolysis. Also a component of the RNA degradosome. The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Interacts with the C-terminal region of the endoribonuclease RNase EIn the RNA degradosome. Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm,Is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the bacterial cell surface. PMID: 8610017 PMID: 9600841 PMID: 9740056 PMID: 9732527 PMID: 12035760 Detected in acossiation with the inner membrane (sequential biochemical fractionations coupled with high resolution mass spectrometry). PMID: 23230279
References:
PMID: 12035760 PMID: 15003462 PMID: 17242352 PMID: 18337249 PMID: 23230279 PMID: 8610017 PMID: 9600841 PMID: 9732527 PMID: 9740056
Pseudogene/Mobile Element:
-

mRNA molec/cell:
21

Proteomics:
PMID: 12624733 PMID: 12488465 PMID: 17137328 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 16858726 PMID: 19767571 PMID: 20521846 PMID: 15115803 PMID: 20932056 PMID: 17446557 PMID: 18425732
Proteomics / Inner Membrane fraction:
PMID: 17309111

Protein molec/cell:
567
PaxDb:
3361 ppm

Class:
Alpha and beta proteins (a+b)
SCOP: 53931
Fold:
Enolase N-terminal domain-like SCOP: 54825
Super Family:
Enolase C-terminal domain-like
SCOP: 51604
Enolase N-terminal domain-like
SCOP: 54826

Go to Complexes

UniProt Name:
Putative polysaccharide export protein Wza
Localization:
Outer Membrane Lipoprotein, Peripheral outer membrane protein facing the extra-cellular space
Notes:
Has a helical structure that crosses membrane. The transmembrane region of Wza is an alpha-helical barrel. Proven pignal peptidase II substrate. It has been demostrated that it can be also secreted and be surface exposed. PMID: 15174130
References:
PMID: 10619844 PMID: 15174130 PMCID: PMC3315050
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 20222674 PMID: 15115803
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0.366 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Minor curlin subunit
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Curli component. CsgB localization requires at least one component of the curli secretion apparatus, CsgF. Curli are a functional amyloid whose in vivo polymerization requires a dedicated nucleator protein, CsgB, and an assembly protein, CsgF. Without CsgF, curli subunits are released from the cell into the media and are inefficiently polymerized, resulting in fewer and mislocalized curli fibers. PMID: 19131513 PMID: 9383186 PMID: 9312041
References:
PMID: 16704339 PMID: 19131513 PMID: 21645131 PMID: 9312041 PMID: 9383186 PMCID: PMC2630086
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19348461
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0.693 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Curli production assembly/transport component CsgF
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Curli component. CsgF is secreted to the cell surface, where it mediates the cell-association and protease-resistance of the CsgB nucleator, suggesting that CsgF is required for specific localization and/or chaperoning of CsgB for full nucleator activity. Curli are a functional amyloid whose in vivo polymerization requires a dedicated nucleator protein, CsgB, and an assembly protein, CsgF. Without CsgF, curli subunits are released from the cell into the media and are inefficiently polymerized, resulting in fewer and mislocalized curli fibers. PMID: 19131513 PMID: 9928475
References:
PMID: 16522795 PMID: 16704339 PMID: 19131513 PMID: 21645131 PMID: 9928475
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
-
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Curli production assembly/transport component CsgG
Localization:
Outer Membrane Lipoprotein, Peripheral outer membrane protein facing the extra-cellular space
Notes:
Curli component. Proven signal peptidase II substrate. CsgG is an outer membrane protein required for the secretion of the two curli structural subunits CsgA and CsgB. CsgG is a lipoprotein that spans the outermembrane and assembles into an oligomeric annular-shaped structure with an inner diameter of approximately 2 nm (Margery L. Evans and Matthew R. Chapman in press). Overexpression of CsgG results in increased sensitivity to the small antibiotic erythromycin (740Da) but not the larger vancomycin (1440Da) suggesting that CsgG has a pore-like activity (Robinson et al 2006). PMID: 15174130
References:
PMID: 15174130 PMID: 16420357 PMID: 16704339 PMID: 19131513 PMID: 21645131
Pseudogene/Mobile Element:
-

mRNA molec/cell:
1

Proteomics:
PMID: 17595003
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
2
PaxDb:
22.4 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Flagellar hook-associated protein 2 (HAP2) (Filament cap protein) (Flagellar cap protein)
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Filament capping protein. PMID: 7551038 PMID: 1527488 PMID: 6305924
References:
PMID: 1527488 PMID: 6305924 PMID: 7551038
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 19767571
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
45.4 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Major curlin subunit
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Curli component. CsgA, is secreted from the cell in an unpolymerized form PMID: 11823641 The secretion and stability of CsgA and CsgB are dependent on the outer membrane lipoprotein CsgG. PMID: 21645131 Curli are a functional amyloid whose in vivo polymerization requires a dedicated nucleator protein, CsgB, and an assembly protein, CsgF. Without CsgF, curli subunits are released from the cell into the media and are inefficiently polymerized, resulting in fewer and mislocalized curli fibers. PMID: 19131513 PMID: 9383186 PMID: 9312041 During a process called interbacterial complementation, a csgB mutant cell secretes soluble CsgA that can be assembled on the surface of a cell expressing only csgB PMID: 8817489 High levels of both IbsC and ShoB lead to changes in membrane potential suggesting that both act at the membrane, consistent with the hydrophobic nature of the proteins.
References:
PMID: 11823641 PMID: 16704339 PMID: 18710431 PMID: 19131513 PMID: 21645131 PMID: 8817489 PMID: 9312041 PMID: 9383186
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
-
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Flagellar hook-associated protein 3 (HAP3) (Hook-filament junction protein)
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Second hook-filament junction protein. PMID: 12730325
References:
PMID: 12631703 PMID: 12730325
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 19767571 PMID: 17446557
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
67.6 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
Phase 1 flagellin SCOP: 64517
Super Family:
Phase 1 flagellin
SCOP: 64518

Go to Complexes

UniProt Name:
Uncharacterized fimbrial-like protein YadC
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Potential fimbrial yad operon (class ??4); Potential tip-adhesin.
References:
PMID: 19820722 PMID: 20345943
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
-
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0.016 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Common fold of diphtheria toxin/transcription factors/cytochrome f SCOP: 49379
Super Family:
Bacterial adhesins
SCOP: 49401

Go to Complexes

UniProt Name:
Flagellar hook-associated protein 1 (HAP1)
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Part of FlgN-FlgK-FliJ-FlhA complex. First hook-filament junction protein. Flagella proteins contribute to the production of outer membrane vesicles. Analysis of E. coli W3110 OMVs revealed that they contain abundant levels of FliC. Compared to the parental strain expressing wild-type flgK, an E. coli strain with a flgK-null mutation produced reduced amounts of OMVs. PMID: 12730325
References:
PMID: 12631703 PMID: 12730325 PMID: 22233518 PMID: 24134841
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 16606699 PMID: 19767571 PMID: 17446557
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
56.2 ppm

Class:
Multi-domain proteins (alpha and beta)
SCOP: 56572
Fold:
Phase 1 flagellin SCOP: 64517
Super Family:
Phase 1 flagellin
SCOP: 64518

Go to Complexes

UniProt Name:
Major outer membrane prolipoprotein Lpp [Cleaved into: Major outer membrane lipoprotein Lpp (Braun lipoprotein) (Murein-lipoprotein)]
Localization:
Outer Membrane Lipoprotein, Peripheral outer membrane protein facing the extra-cellular space
Notes:
Trigger factor-sensitive aggregation. Proven pignal peptidase II substrate. Outer membrane protein determined by 2D gel electrophoresis (Lopez-Campistrous et al 2005). Covalently attached to the peptidoglycan cell wall by the ??-amino group of its C-terminal Lys residue; stabilizes the bacterial envelope. Identified in nucleoids collected by sucrose gradient centrifugation and analyzed by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). PMID: 21541338 PMID: 4575979
References:
PMID: 15174130 PMID: 15911532 PMID: 16079137 PMID: 19737520 PMID: 21219470 PMID: 21541338 PMID: 3013869 PMID: 4575979
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
PMID: 12488465 PMID: 19348461 PMID: 20222674 PMID: 16967446 PMID: 16858726 PMID: 19767571 PMID: 16079137 PMID: 15115803 PMID: 20932056 PMID: 19343722 PMID: 20923772
Proteomics / Inner Membrane fraction:
PMID: 16079137 PMID: 17309111

Protein molec/cell:
-
PaxDb:
6110 ppm

Class:
Coiled coil proteins
SCOP: 57942
Fold:
Parallel coiled-coil SCOP: 57943
Super Family:
Outer membrane lipoprotein
SCOP: 58042

Go to Complexes

UniProt Name:
Basal-body rod modification protein FlgD
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Hook-capping protein. The hook cap FlgD is displaced by FlgK, allowing filament growth PMID: 12631703 Using the hook scaffolding protein FlgD of Escherichia coli as a model substrate, it is demonstrated that the export signal is contained within the N-terminal 71 amino acids of FlgD. PMID: 16897036 PMID: 16897036
References:
PMID: 12631703 PMID: 16897036
Pseudogene/Mobile Element:
pseudogene (Ochman & Davalos, 2006)

mRNA molec/cell:
-

Proteomics:
-
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0 ppm

Class:
-
Fold:
-
Super Family:
-

Go to Complexes

UniProt Name:
Flagellar hook protein FlgE
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Hook protein. PMID: 12730325
References:
PMID: 12631703 PMID: 12730325
Pseudogene/Mobile Element:
pseudogene (Ochman & Davalos, 2006)

mRNA molec/cell:
-

Proteomics:
PMID: 19767571 PMID: 18796603
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
17.2 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Flagellar hook protein flgE SCOP: 117142
Super Family:
Flagellar hook protein flgE
SCOP: 117143

Go to Complexes

UniProt Name:
Uncharacterized fimbrial-like protein YdeS
Localization:
Peripheral outer membrane protein facing the extra-cellular space
Notes:
Potential fimbrial yde operon (class ??1); Fimbrial Subunit. Disulfide bridge (38 78)
References:
PMID: 19820722 PMID: 20345943
Pseudogene/Mobile Element:
-

mRNA molec/cell:
-

Proteomics:
-
Proteomics / Inner Membrane fraction:
-

Protein molec/cell:
-
PaxDb:
0.032 ppm

Class:
All beta proteins
SCOP: 48724
Fold:
Common fold of diphtheria toxin/transcription factors/cytochrome f SCOP: 49379
Super Family:
Bacterial adhesins
SCOP: 49401

Go to Complexes