TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.B.12.1.1









Autotransporter of adhesin involved in diffuse adherence, AidA (Charbonneau and Mourez, 2007). Heptosylated on 16 ser and thr residues which is required for adhesion (Charbonneau et al., 2007).
Bacteria
Proteobacteria
AidA of E. coli
*1.B.12.1.2









Autoexporter of virulence factor G, VirG or IcsA
Bacteria
Proteobacteria
VirG of Shigella flexneri
*1.B.12.1.3









The MisL autotransporter/fibronectin binding protein; expression of misL is regulated by MisT (Tükel et al., 2007)

Bacteria
Proteobacteria
MisL of Salmonella typhimurium (AAD16954)
*1.B.12.1.4









Putative autotransporter, YcbB; YuaO of 1758 aas.

Bacteria
Proteobacteria
YuaO of E. coli K12
*1.B.12.1.5









Biofilm adhesin autotransporter of 1250 aas, YfaL (Berry et al. 2009).

Bacteria
Proteobacteria
YfaL of E. coli
*1.B.12.1.6









Autotransporter of 1349 aas, EhaA, involved in autoaggregation, biofilm formation and adhesion to epithelial cells (Wells et al. 2008).

Bacteria
Proteobacteria
EhaA of E. coli O157
*1.B.12.1.7









Autotransporter PmpA of 975 aas (Vasilevsky et al. 2016).

Bacteria
Chlamydiae
PmpA of Chlamydia trachomatis
*1.B.12.1.8









PmpB of 1754 aas (Vasilevsky et al. 2016)

Bacteria
Chlamydiae
PmpB of Chlamydia trachomatis
*1.B.12.1.9









PmpD of 1531 aas (Vasilevsky et al. 2016).

Bacteria
Chlamydiae
PmpD of Chlamydia trachomatis
*1.B.12.1.10









PmpF of 1034 aas (Vasilevsky et al. 2016).

Bacteria
Chlamydiae
PmpF of Chlamydia trachomatis
*1.B.12.2.1









Autoexporter of pertactin, Ptt of 910 aas with a C-terminal β-barrel domain which has been crystalized (Zhu et al. 2007).  It is a bacterial adhesin and vaccine target which influences the duration of B. pertussis infections but does not otherwise affect the disease (Vodzak et al. 2016).

Bacteria
Proteobacteria
Ptt of Bordetella pertussis
*1.B.12.2.2









Autoexporter of tracheal colonization factor
Bacteria
Proteobacteria
TcfA of Bordetella pertussis
*1.B.12.2.3









Autoexporter of Bordetella resistance to killing proteins
Bacteria
Proteobacteria
BrkA of Bordetella pertussis
*1.B.12.2.4









Autotransporter-1 family member

Bacteria
Firmicutes
Autotransporter-1 of Selenomonas sputigena
*1.B.12.2.5









Autotransporter, BapC of 909 aas with an established transmembrane β-barrel and a long α-structured passenger domain (Riaz et al. 2015).

Bacteria
Proteobacteria
BapC of Bordetella pertussis
*1.B.12.2.6









Putative autotransporter of 955 aas

Bacteria
Proteobacteria
Autotransporter of E. coli
*1.B.12.2.7









Autotransporter of 980 aas, EhaB, involved in biofilm formation as well as adhesion to collagen I and laminin (Wells et al. 2008).

Bacteria
Proteobacteria
EhaB of E. coli
*1.B.12.3.1









Autoexporter of IgA protease
Bacteria
Proteobacteria
IgA protease of Neisseria gonorrhoeae
*1.B.12.3.2









Autoexporter of adhesion and penetration protein

Bacteria
Proteobacteria
Hap of Haemophilus influenzae
*1.B.12.4.1









Autoexporter of EPEC-secreted protein C
Bacteria
Proteobacteria
EspC of E. coli
*1.B.12.4.2









Autoexporter of temperature-sensitive hemagglutinin, a hemoglobin binding protease, Tsh/Hbp (1377 aas) (Jong and Luirink, 2008; Peterson et al., 2006). The pore of the Hbp TD is largely obstructed, but a variant that lacked one amino acid residue from the N-terminus showed the opening and closing of a channel comparable to what was reported for the TD of NalP. Hbp is processed by an autocatalytic intramolecular mechanism resulting in the stable docking of the α-helical plug in the barrel.

Bacteria
Proteobacteria
Tsh/Hbp of E. coli
*1.B.12.4.3









Autotransporter of serine protease, EspP (with long N-terminal leader that prevents improper folding in the periplasm) (Szabady et al., 2005; Ieva et al., 2008). Energy for export is provided by the folding of the C-terminal domain (Peterson et al., 2010).

Bacteria
Proteobacteria
EspP of E. coli (NP_052685)
*1.B.12.4.4









Autotransporter-1, Pet (serine protease; 1295 aas)) (Eslava et al., 1998Leyton et al., 2010).  The first stage of autotransporter folding determines whether subsequent translocation can deliver the N-terminal domain to its functional form on the bacterial cell surface. Paired conserved glycine-aromatic 'mortise and tenon' motifs join neighbouring beta-strands in the C-terminal barrel domain, and mutations within these motifs slow the rate and extent of passenger domain translocation to the surface of bacterial cell (Leyton et al. 2014).

Bacteria
Proteobacteria
Pet of E. coli (O68900)
*1.B.12.4.5









Autotransporter-1, Pic (serine protease;1372 aas) (Henderson et al., 1999).

Bacteria
Proteobacteria
Pic of E. coli (Q7BS42)
*1.B.12.4.6









Autotransporter-1, Sat (Serine protease; 1295 aas) (Guyer et al., 2000).

Bacteria
Proteobacteria
Sat of E. coli (Q8FDW4)
*1.B.12.4.7









Vacuolating Autotransporter-1, Vat (1376 aas; protease; pertactin-like passenger domain; virulence factor)

Bacteria
Proteobacteria
Vat of E. coli (A1A7W8)
*1.B.12.5.1









Autoexporter of serine protease
Bacteria
Proteobacteria
Ssp of Serratia marcescens
*1.B.12.5.2









The Azorhizobial autotransporter AoaA, required for N- fixing activity of stem nodules (Suzuki et al., 2008).
Bacteria
Proteobacteria
AoaA of Azorhizobium caulinodans (A8IBA8)
*1.B.12.5.3









The cytotoxin/agglutinin AT-1 protein, Pta (Alamuri and Mobley, 2008).
Bacteria
Proteobacteria
Pta of Proteus mirabilis (B4F2I9)
*1.B.12.5.4









Autotransporter-1, ShdA (2035 aas) (Kingsley et al., 2003).

Bacteria
Proteobacteria
ShdA of Salmonella enterica (Q9XCJ4)
*1.B.12.5.5









Autotransporter-1, BigA (1953 aas) (Lauri et al. 2011).

Bacteria
Proteobacteria
BigA of Salmonella typhimurium (P25927)
*1.B.12.5.6









Autotransporter essential for virulence and biofilm formation of 1242 aas, Pfa1.  The passenger domain is a serine protease, cytotoxic to cultured fish cells (Hu et al. 2009).

Bacteria
Proteobacteria
Pfa1 of Pseudomonas fluorescens
*1.B.12.5.7









Putative autotransporter of 886 aas

Bacteria
Proteobacteria
AT of Bordetella pertussis
*1.B.12.5.8









Autotransporter of 1128 aas

Bacteria
Proteobacteria
AT of Chromobacterium vioalceum
*1.B.12.5.9









Autoexporter of lipase/esterase, EstA
Bacteria
Proteobacteria
EstA of Pseudomonas aeruginosa
*1.B.12.5.10









Autotransporter, YapE of 1072 aas (Lawrenz et al. 2013).

Bacteria
Proteobacteria
YapE of Yersinia pestis
*1.B.12.5.11









Autotransporter outer membrane beta-barrel domain-containing protein of 2358 aa

Bacteria
Proteobacteria
Autotransporter outer membrane beta-barrel domain-containing protein of Burkholderia cepacia
*1.B.12.6.1









Autoexporter of vacuolating cytotoxin, VacA or Vac2, of 1287 aas.

Bacteria
Proteobacteria
VacA of Helicobacter pylori
*1.B.12.7.1









Autoexporter of Helicobacter surface ring protein
Bacteria
Proteobacteria
Hsr of Helicobacter mustelae
*1.B.12.8.1









Putative autotransporter of 736 aas

Bacteria
Proteobacteria
AT of Yersina pestis
*1.B.12.8.2









Fluffing protein (Flu) or antigen-43 (Ag-43; Ag43; also called YeeQ and YzzX). Processed proteolytically to the α- (soluble) and β- (membrane anchored) subunits; determines colony morphology and autoaggregation of E. coli K12 and many pathogenic strains (Henderson et al., 1997; Klemm et al. 2006).  May function in autotransporter processing.

Bacteria
Proteobacteria
Flu of E. coli
*1.B.12.8.3









Autotransporter-1, TibA (989 aas; an Adhesin/Invasin associated with some enterotoxigenic E. coli) (Lindenthal and Elsinghorst et al., 1999; Klemm et al. 2006Klemm et al. 2006).

Bacteria
Proteobacteria
TibA of E. coli (Q9XD84)
*1.B.12.9.1









Autotransporter of N-terminal protease passenger domain that cleaves surface-localized virulence factors.  The 3-d structure is known (Oomen et al., 2004). The crystal structure of the NalP translocator domain revealed a transmembrane beta-barrel containing a central alpha-helix. The transmembrane beta-barrel is stable even in the absence of the alpha-helix. Removal of the helix results in an influx of water into the pore region, suggesting the helix acts as a 'plug' (Khalid and Sansom 2006). The dimensions of the pore fluctuate, but the NalP monomer is sufficient for the transport of the passenger domain in an unfolded or extended conformation (Khalid and Sansom 2006). NalP is subject to phase variation (Oldfield et al. 2013).

Bacteria
Proteobacteria
pNalP of Neisseria meningitidis (AAN71715)
*1.B.12.9.2









The serine protease autotransporter, SphB1
Bacteria
Proteobacteria
SphB1 of Bordetella pertussis (Q7W0C9)
*1.B.12.10.1









The Campylobacter adhesion protein, CapA (Ashgar et al., 2007)
Bacteria
Proteobacteria
CapA of Campylobacter jejuni (Q0PAN9)
*1.B.12.11.1









The outer membrane acid phosphatase autotransporter, MapA (940 aas) (Hoopman et al., 2008)
Bacteria
Proteobacteria
MapA of Moraxella catarrhalis (A9XED4)
*1.B.12.12.1









The acidic repeat AT protein, ARP (1441 aas) (Litwin et al., 2007) (shows N-terminal sequence similarity to 1.B.12.2.3 and C-terminal similarity to 1.B.12.8.2).
Bacteria
Proteobacteria
Arp of Bartonella henselae (Q6G2D1)
*1.B.12.13.1









Surface antigen, Sca2; required for intracellular actin based motility in Rickettsia (Kleba et al., 2010).

Bacteria
Proteobacteria
Sca2 of Rickettsia rickettsii (Q3L8P4)
*1.B.12.13.2









Autotransporter, OmpA

Bacteria
Proteobacteria
OmpA of Rickettsia sp. p1A (B5A5W2)
*1.B.12.13.3









Autotransporter, OmpB

Bacteria
Proteobacteria
OmpB of Rickettsia helvetica (F1CET6)