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TCID	Name	Domain	Kingdom/Phylum	Protein(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	Pseudomonadota	AidA of E. coli
1.B.12.1.2	Autoexporter of virulence factor G, VirG or IcsA	Bacteria	Pseudomonadota	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	Pseudomonadota	MisL of Salmonella typhimurium (AAD16954)
1.B.12.1.4	Putative autotransporter, YcbB; YuaO of 1758 aas.	Bacteria	Pseudomonadota	YuaO of E. coli K12
1.B.12.1.5	Biofilm adhesin autotransporter of 1250 aas, YfaL (Berry et al. 2009).	Bacteria	Pseudomonadota	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	Pseudomonadota	EhaA of E. coli O157
1.B.12.1.7	Autotransporter PmpA of 975 aas (Vasilevsky et al. 2016).	Bacteria	Chlamydiota	PmpA of Chlamydia trachomatis
1.B.12.1.8	PmpB of 1754 aas (Vasilevsky et al. 2016)	Bacteria	Chlamydiota	PmpB of Chlamydia trachomatis
1.B.12.1.9	PmpD of 1531 aas (Vasilevsky et al. 2016).	Bacteria	Chlamydiota	PmpD of Chlamydia trachomatis
1.B.12.1.10	PmpF of 1034 aas (Vasilevsky et al. 2016).	Bacteria	Chlamydiota	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	Pseudomonadota	Ptt of Bordetella pertussis
1.B.12.2.2	Autoexporter of tracheal colonization factor	Bacteria	Pseudomonadota	TcfA of Bordetella pertussis
1.B.12.2.3	Autoexporter of Bordetella resistance to killing proteins	Bacteria	Pseudomonadota	BrkA of Bordetella pertussis
1.B.12.2.4	Autotransporter-1 family member	Bacteria	Bacillota	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	Pseudomonadota	BapC of Bordetella pertussis
1.B.12.2.6	Putative autotransporter of 955 aas	Bacteria	Pseudomonadota	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	Pseudomonadota	EhaB of E. coli
1.B.12.3.1	Autoexporter of IgA protease	Bacteria	Pseudomonadota	IgA protease of Neisseria gonorrhoeae
1.B.12.3.2	Autoexporter of adhesion and penetration protein	Bacteria	Pseudomonadota	Hap of Haemophilus influenzae
1.B.12.3.3	Autotransporter/adhesin of 912 aas and 1 N-terminal TMS, Aae. Aae mediates A. actinomycetemcomitans adhesion to epithelial cells and may be involved in biofilm formation and interaction with adsorbed salivary proteins (Nunes et al. 2017).	Bacteria	Pseudomonadota	Aae of Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
1.B.12.4.1	Autoexporter of EPEC-secreted protein C	Bacteria	Pseudomonadota	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	Pseudomonadota	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	Pseudomonadota	EspP of E. coli (NP_052685)
1.B.12.4.4	Autotransporter-1, Pet (serine protease; 1295 aas)) (Eslava et al., 1998; Leyton 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	Pseudomonadota	Pet of E. coli (O68900)
1.B.12.4.5	Autotransporter-1, Pic (serine protease;1372 aas) (Henderson et al., 1999).	Bacteria	Pseudomonadota	Pic of E. coli (Q7BS42)
1.B.12.4.6	Autotransporter-1, Sat (Serine protease; 1295 aas) (Guyer et al., 2000).	Bacteria	Pseudomonadota	Sat of E. coli (Q8FDW4)
1.B.12.4.7	Vacuolating Autotransporter-1, Vat (1376 aas; protease; pertactin-like passenger domain; virulence factor)	Bacteria	Pseudomonadota	Vat of E. coli (A1A7W8)
1.B.12.5.1	Autoexporter of serine protease	Bacteria	Pseudomonadota	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	Pseudomonadota	AoaA of Azorhizobium caulinodans (A8IBA8)
1.B.12.5.3	The cytotoxin/agglutinin AT-1 protein, Pta (Alamuri and Mobley, 2008).	Bacteria	Pseudomonadota	Pta of Proteus mirabilis (B4F2I9)
1.B.12.5.4	Autotransporter-1, ShdA (2035 aas) (Kingsley et al., 2003).	Bacteria	Pseudomonadota	ShdA of Salmonella enterica (Q9XCJ4)
1.B.12.5.5	Autotransporter-1, BigA (1953 aas) (Lauri et al. 2011).	Bacteria	Pseudomonadota	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	Pseudomonadota	Pfa1 of Pseudomonas fluorescens
1.B.12.5.7	Putative autotransporter of 886 aas	Bacteria	Pseudomonadota	AT of Bordetella pertussis
1.B.12.5.8	Autotransporter of 1128 aas	Bacteria	Pseudomonadota	AT of Chromobacterium vioalceum
1.B.12.5.9	Autoexporter of lipase/esterase, EstA	Bacteria	Pseudomonadota	EstA of Pseudomonas aeruginosa
1.B.12.5.10	Autotransporter, YapE of 1072 aas (Lawrenz et al. 2013).	Bacteria	Pseudomonadota	YapE of Yersinia pestis
1.B.12.5.11	Autotransporter outer membrane beta-barrel domain-containing protein of 2358 aa	Bacteria	Pseudomonadota	Autotransporter outer membrane beta-barrel domain-containing protein of Burkholderia cepacia
1.B.12.7.1	Autoexporter of Helicobacter surface ring protein	Bacteria	Campylobacterota	Hsr of Helicobacter mustelae
1.B.12.8.1	Putative autotransporter of 736 aas	Bacteria	Pseudomonadota	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	Pseudomonadota	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. 2006 Klemm et al. 2006).	Bacteria	Pseudomonadota	TibA of E. coli (Q9XD84)
1.B.12.8.4	Putative outer membrane autotransporter, YnaI, of 863 aas and one N-terminal TMS.	Bacteria	Pseudomonadota	YnaI of E. coli
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 12 β-stranded 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	Pseudomonadota	pNalP of Neisseria meningitidis (AAN71715)
1.B.12.9.2	The serine protease autotransporter, SphB1	Bacteria	Pseudomonadota	SphB1 of Bordetella pertussis (Q7W0C9)
1.B.12.10.1	The Campylobacter adhesion protein, CapA (Ashgar et al., 2007)	Bacteria	Campylobacterota	CapA of Campylobacter jejuni (Q0PAN9)
1.B.12.11.1	The outer membrane acid phosphatase autotransporter, MapA (940 aas) (Hoopman et al., 2008)	Bacteria	Pseudomonadota	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	Pseudomonadota	Arp of Bartonella henselae (Q6G2D1)
1.B.12.12.4	Uncharacterized opacity protein or related surface antigen of 398 aas and 1 N-terminal TMS.	Bacteria	Planctomycetota	UP of Candidatus Brocadiaceae bacterium
1.B.12.13.1	Surface antigen, Sca2; required for intracellular actin based motility in Rickettsia (Kleba et al., 2010).	Bacteria	Pseudomonadota	Sca2 of Rickettsia rickettsii (Q3L8P4)
1.B.12.13.2	Autotransporter, OmpA	Bacteria	Pseudomonadota	OmpA of Rickettsia sp. p1A (B5A5W2)
1.B.12.13.3	Autotransporter, OmpB	Bacteria	Pseudomonadota	OmpB of Rickettsia helvetica (F1CET6)