TCID | Name | Domain | Kingdom/Phylum | Protein(s) | ||||
---|---|---|---|---|---|---|---|---|
1.B.48.1.1 | The 36 β-stranded outer membrane porin, CsgG with auxiliary subunits, CsgE and CsgF (Goyal et al. 2014). Curli are functional amyloid fibres that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria (predominantly of the α and γ classes). They provide a fitness advantage in pathogenic strains and induce a strong pro-inflammatory response during bacteraemia. Curli formation requires a dedicated protein secretion machinery comprising the outer membrane lipoprotein CsgG and two soluble accessory proteins, CsgE and CsgF. Curli formation requires a dedicated protein secretion machinery comprising the outer membrane lipoprotein CsgG and two soluble accessory proteins, CsgE and CsgF. Goyal et al. 2014 reported the X-ray structure of Escherichia coli CsgG in a non-lipidated, soluble form as well as in its native membrane-extracted conformation. CsgG forms an oligomeric transport complex composed of nine anticodon-binding-domain-like units that give rise to a 36-stranded β-barrel that traverses the bilayer and is connected to a cage-like vestibule in the periplasm. The transmembrane and periplasmic domains are separated by a 0.9-nm channel constriction composed of three stacked concentric phenylalanine, asparagine and tyrosine rings that may guide the extended polypeptide substrate through the secretion pore. The specificity factor CsgE forms a nonameric adaptor that binds and closes off the periplasmic face of the secretion channel, creating a 24,000 Å pre-constriction chamber. The structural, functional and electrophysiological analyses imply that CsgG is an ungated, non-selective protein secretion channel that is expected to employ a diffusion-based, entropy-driven transport mechanism (Goyal et al. 2014). SuFEx chemistry for cross-linking enables covalent assembly of a 280-kDa 18-subunit pore-forming complex used for DNA sequencing (Schnaider et al. 2024). | Bacteria |
Pseudomonadota | CsgEFG of E. coli | ||||
1.B.48.1.2 | Curli assembly/transport compenent, CsgG. (TolB-N Superfamily of CDD) | Bacteria |
Chlorobiota | CsgG of Chlorobium phaeobacteroides | ||||
1.B.48.1.3 | CsgG homologue | Bacteria |
Cyanobacteriota | CsgG homologue of Synechococcus sp. JA-2-3B'a(2-13) | ||||
1.B.48.1.4 | CsgG homologue | Bacteria |
Deinococcota | CsgG homologue of Thermus thermophilus
| ||||
1.B.48.1.5 | CsgG homologue of 272 aas | Bacteria |
Pseudomonadota | CsgG homologue of Glaciecola nitratireducens | ||||
1.B.48.1.6 | CsgG homologue of 347 aas | Bacteria |
Bacillota | CsgG homologue of Halobacteroides halobius | ||||
1.B.48.1.7 | Putative lipoprotein of 187 aas | Bacteria |
Spirochaetota | Putative lipoprotein of Leptospira interrogans | ||||
1.B.48.1.8 | Uncharacterized protein of 303 aas | Bacteria |
Thermodesulfobacteriota | UP of Desulfarculus baarsii | ||||
1.B.48.1.9 | CsgG homologue of 485 aas | Bacteria |
Spirochaetota | CsgG homologue of Leptospira interrogans | ||||
1.B.48.1.10 | Uncharacterized protein of 248 aas | Bacteria |
Spirochaetota | UP of Leptospira biflexa | ||||
1.B.48.1.11 | Putative porin of 333 aas and 1 N-terminal TMS | Bacteria |
Bdellovibrionota | PP of Bdellovibrio exovorus | ||||
1.B.48.2.1 | Putative porin of 394 aas | Bacteria |
Thermotogota | Porin of Thermosipho melanesiensis | ||||
1.B.48.2.2 | Putative curli porin, CgsG of 489 aas | Bacteria |
Spirochaetota | CgsG of Brachyspira pilosicoli | ||||
1.B.48.2.3 | CsgG homologue of 412 aas | Bacteria |
Thermotogota | CsgG homologue of Marinitoga piezophila | ||||
1.B.48.2.4 | CsgG homologue of 399 aas | Bacteria |
Aquificota | CsgG homologue of Persephonella marina | ||||
1.B.48.2.5 | Uncharacterized protein of 275 aas | Bacteria |
Bacteroidota | UP of Bacteroides xylanisolvens | ||||
1.B.48.2.6 | Uncharacterized protein of 588 aas | Bacteria |
Thermotogota | UP of Thermosipho melanesiensis | ||||
1.B.48.3.1 | Protein with N-terminal CsgG domain and two central PEGA domains (similar to beta-barrel S-layer domains of 464 aas. | Bacteria |
Spirochaetota | CsgG/PEGA protein of Spirochaeta thermophila | ||||
1.B.48.3.2 | Protein with N-terminal CsgG domain, central PEGA domain and C-terminal autotransporter domain of 422 aas. The PEGA domain (residues 160 - 220) is found in the OMR Ferripyochelin receptor, FptA (1.B.14.1.8), repeated at least 3 times every ~36 aas. | Bacteria |
Spirochaetota | Uncharacterized protein of Turneriella parva (Leptospira parva) | ||||
1.B.48.3.3 | Putative adenylate cyclase of 478 aas with N-terminal CsgG domain. | Bacteria |
Myxococcota | Uncharacterized protein of Myxococcus stipitatus | ||||
1.B.48.3.4 | S-layer-like β-barrel domain protein of 527aas and 2 N- and C-terminal TMSs. | Bacteria |
Spirochaetota | S-layer-like protein of Leptospira interrogans (Q8F8C2) | ||||
1.B.48.4.1 | CsgG homologue of 397 aas | Bacteria |
Aquificota | CsgG homologue of Thermovibrio ammonificans | ||||
1.B.48.4.2 | Uncharacterized protein of 430 aas | Bacteria |
Pseudomonadota | UP of Alcanivorax borkumensis | ||||
1.B.48.5.1 | Uncharacterized protein, YcfM of 196 aas | Bacteria |
Pseudomonadota | YcfM of Vibrio parahaemolyticus | ||||
1.B.48.6.1 | Uncharacterized protein of 448 aas | Bacteria |
Spirochaetota | UP of Treponema denticola |