Exclusively T3SE Pfam domains collected from T3SEs are presented in the database, displaying domain name, Pfam ID, host and possible function.

Name ID Host Function
ADPrib_exo_Tox PF03496.9 Animals This is a family of bacterial and viral bi-glutamic acid ADP-ribosyltransferases, where, in Q93Q17 E403 is the catalytic residue and E401 contributes to the transfer of ADP-ribose to the target protein. In clostridial species it is actin that is being ADP-ribosylated; this result is lethal and dermonecrotic in infected mammals.
ART PF01129.13 Plants NAD(P)+-protein-arginine ADP-ribosyltransferase.
Avirulence PF03377.8 Plants Unknown
AvrB_AvrC PF05394.6 Plants This family consists of several avirulence proteins from Pseudomonas syringae and Xanthomonas campestris.
AvrD PF05655.6 Plants This family consists of several avirulence D (AvrD) proteins primarily found in Pseudomonas syringae.
AvrE PF11725.3 Plants This family is secreted by gram-negative Gammaproteobacteria such as Pseudomonas syringae of tomato and the fire blight Plants pathogen Erwinia amylovora, amongst others. It is an essential pathogenicity factor of approximately 198 kDa. Its injection into the host-Plants is dependent upon the bacterial type III or Hrp secretion system. The family is long and carries a number of predicted functional regions, including an ERMS or endoplasmic reticulum membrane retention signal at both the C- and the N-termini, a leucine-zipper motif from residues 539-560, and a nuclear localisation signal at 1358-1361. this conserved AvrE-family of effectors is among the few that are required for full virulence of many phytopathogenic pseudomonads, erwinias and pantoeas.
AvrPphF-ORF-2 PF09143.5 Plants Members of this family of Plants pathogenic proteins adopt an elongated structure somewhat reminiscent of a mushroom that can be divided into 'stalk' and 'head' subdomains. The stalk subdomain is composed of the N-terminal helix (alpha1) and beta strands beta3-beta4. An antiparallel beta sheet (beta5, beta7-beta8) forms the base of the head subdomain that interacts with the stalk. A pair of twisted antiparallel beta sheets (beta1 and beta6; beta2 and beta9/9') supported by alpha2 form the dome of the head. The head subdomain possesses weak structural similarity with the catalytic portion of a number of ADP-ribosyltransferase toxins.
AvrPtoB-E3_ubiq PF09046.5 Plants The E3 ubiquitin ligase domain found in the bacterial protein AvrPtoB inhibits immunity-associated programmed cell death (PCD) when translocated into Plants cells, probably by recruiting E2 enzymes and transferring ubiquitin molecules to cellular proteins involved in regulation of PCD and targeting them for degradation. The structure of this domain reveals a globular fold centred on a four-stranded beta-sheet that packs against two helices on one face and has three very extended loops connecting the elements of secondary structure, with remarkable homology to the RING-finger and U-box families of proteins involved in ubiquitin ligase complexes in eukaryotes.
CNF1 PF05785.7 Animals This family consists of several bacterial cytotoxic necrotizing factor proteins as well as related dermonecrotic toxin (DNT) from Bordetella species. Cytotoxic necrotizing factor 1 (CNF1) causes necrosis of rabbit skin and re-organisation of the actin cytoskeleton in cultured cells. Bordetella dermonecrotic toxin (DNT) stimulates the assembly of actin stress fibres and focal adhesions by deamidating or polyaminating Gln63 of the small GTPase Rho. DNT is an A-B toxin which is composed of an N-terminal receptor-binding (B) domain and a C-terminal enzymatically active (A) domain.
DUF1076 PF06416.7 Animals This family consists of several hypothetical bacterial proteins exclusive to Escherichia coli and Salmonella typhi. The function of this family is unknown.
DUF1537 PF07005.6 Plants This conserved region is found in proteins of unknown function in a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis.
DUF1547 PF07577.6 Animals This family appears to be found only in a small family of Chlamydia species.
DUF720 PF05302.6 Animals This family consists of several uncharacterised Chlamydia proteins of unknown function.
Effector_1 PF04518.7 Animals This is a family of effector proteins which are secreted by the type III secretion system. The precise function of this family is unknown.
EspA PF03433.8 Animals EspA is the prototypical member of this family. EspA, together with EspB, EspD and Tir are exported by a type III secretion system. These proteins are essential for attaching and effacing lesion formation. EspA is a structural protein and a major component of a large, transiently expressed, filamentous surface organelle which forms a direct link between the bacterium and the host cell.
EspB PF05802.6 Animals EspB is a type-III-secreted pore-forming protein of enteropathogenic Escherichia coli (EPEC) which is essential for EPEC pathogenesis. EspB is also found in Citrobacter rodentium.
EspF PF04806.7 Animals The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.
EspG PF06872.6 Animals This family consists of several EspG like proteins from Citrobacter rodentium and Escherichia coli. EspG is secreted by the type III secretory system and is translocated into host epithelial cells. EspG is homologous with Shigella flexneri protein VirA and can rescue invasion in a Shigella virA mutant, indicating that these proteins are functionally equivalent in Shigella. EspG plays an accessory but as yet undefined role in EPEC virulence that may involve intestinal colonisation.
GDPD PF03009.12 Plants E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C PF00388 which suggests that this family may adopt a TIM barrel fold.
Glyco_hydro_12 PF01670.11 Plants Unknown
HopW1-1 PF15457.1 Plants HopW1-1 is a family of bacterial modular P. syringae Avr effectors that induce accumulation of the signal molecule salicylic acid (SA) and the transcripts of HWI1 (HOPW1-1-INDUCED GENE1) in Arabidopsis. Thus HopW1-1 elicits a resistance response in Arabidopsis.
HrpA_pilin PF09589.5 Plants HrpA is an essential component of the type III secretion system (TTSS) which pathogens use to inject virulence factors directly into their host cells, and to cause disease. The TTSS has an Hrp pilus appendage for channelling effector proteins through the Plants cell wall and this pilus elongates by the addition of HrpA pilin subunits at the distal end.
HrpJ PF07201.6 Animals This family represents a conserved region approximately 200 residues long within a number of bacterial hypersensitivity response secretion protein HrpJ and similar proteins. HrpJ forms part of a type III secretion system through which, in phytopathogenic bacterial species, virulence factors are thought to be delivered to Plants cells. This family also includes the InvE invasion protein from Salmonella. This protein is involved in host parasite interactions and mutations in the InvE gene render Salmonella typhimurium non-invasive. InvE S. typhimurium mutants fail to elicit a rapid Ca2+ increase in cultured cells, an important event in the infection procedure and internalisation of S. typhimurium into epithelial cells. This family includes bacterial SepL and SsaL proteins. SepL plays an essential role in the infection process of enterohemorrhagic Escherichia coli and is thought to be responsible for the secretion of EspA, EspD, and EspB. SsaL of Salmonella typhimurium is thought to be a component of the type III secretion system.
IncA PF04156.9 Animals Chlamydia trachomatis is an obligate intracellular bacterium that develops within a parasitophorous vacuole termed an inclusion. The inclusion is non-fusogenic with lysosomes but intercepts lipids from a host cell exocytic pathway. Initiation of chlamydial development is concurrent with modification of the inclusion membrane by a set of C. trachomatis-encoded proteins collectively designated Incs. One of these Incs, IncA, is functionally associated with the homotypic fusion of inclusions. This family probably includes members of the wider Inc family rather than just IncA.
IpaB_EvcA PF03278.8 Animals This family includes IpaB, which is an invasion plasmid antigen from Shigella as well as EvcA from E. coli Q9ZNF1. Members of this family seem to be involved in pathogenicity of some enterobacteria. However the exact function of this component is not clear.
IpaC_SipC PF09599.5 Animals This entry represents a family of proteins associated with bacterial type III secretion systems, which are injection machines for virulence factors into host cell cytoplasm. Characterized members of this protein family are known to be secreted and are described as invasins, including IpaC from Shigella flexneri and SipC from Salmonella typhimurium. Members may be referred to as invasins, pathogenicity island effectors, and cell invasion proteins.
IpaD PF06511.6 Animals This family consists of several invasion plasmid antigen IpaD proteins. Entry of Shigella flexneri into epithelial cells and lysis of the phagosome involve the IpaB, IpaC, and IpaD proteins, which are secreted by type III secretion machinery.
IpgD PF05925.7 Animals This family consists of several enterobacterial IpgD like virulence factor proteins. In the Gram-negative pathogen Shigella flexneri, the virulence factor IpgD is translocated directly into eukaryotic cells and acts as a potent inositol 4-phosphatase that specifically dephosphorylates phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] into phosphatidylinositol 5-monophosphate [PtdIns(5)P] that then accumulates. Transformation of PtdIns(4,5)P(2) into PtdIns(5)P by IpgD is responsible for dramatic morphological changes of the host cell, leading to a decrease in membrane tether force associated with membrane blebbing and actin filament remodelling.
IU_nuc_hydro PF01156.14 Plants Unknown
LcrR PF09621.5 All This family of proteins are encoded within type III secretion operons and have been characterised in Yersinia as a regulator of the Low-Calcium Response (LCR).
Lipase_GDSL PF00657.17 Animals Unknown
LZ_Tnp_IS481 PF13011.1 Animals This is the upstream region of the conjoined ORF AB of insertion element 481. The B portion of the ORF AB carries the transposase activity in family rve.
MaoC_dehydratas PF01575.14 Plants The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.
NEL PF14496.1 Animals This NEL or novel E3 ligase domain is found at the C-terminus of bacterial virulence factors. Its sequence is different from those of the eukaryotic HECT and RING-finger E3 ligases, and it subverts the host ubiquitination process. At the N-terminus of the family-members there is a series of LRR repeats, and the NEL domain interacts with the most N-terminal repeat. The key residue for the ligation step is the cysteine, eg found at position 386 in UniProtKB:E7K2H2. The LRR section sequesters this active site until invasion has occurred.
NolX PF05819.6 Plants This family consists of Rhizobium NolX and Xanthomonas HrpF proteins. The interaction between the Plants pathogen Xanthomonas campestris pv. vesicatoria and its host Plantss is controlled by hrp genes (hypersensitive reaction and pathogenicity), which encode a type III protein secretion system. Among type III-secreted proteins are avirulence proteins, effectors involved in the induction of Plants defence reactions. HrpF is dispensable for protein secretion but required for AvrBs3 recognition in Plantsa, is thought to function as a translocator of effector proteins into the host cell. NolX, a soybean cultivar specificity protein, is secreted by a type III secretion system (TTSS) and shows homology to HrpF of the Plants pathogen Xanthomonas campestris pv. vesicatoria. It is not known whether NolX functions at the bacterium-Plants interface or acts inside the host cell. NolX is expressed in Plantsa only during the early stages of nodule development.
NUDIX PF00293.23 Plants Unknown
Patatin PF01734.17 Animals Family of patatin-like phospholipases consists of various patatin glycoproteins from the total soluble protein from potato tubers, and also some proteins found in vertebrates. Patatin is a storage protein but it also has the enzymatic activity of phospholipase, catalysing the cleavage of fatty acids from membrane lipids.
Pec_lyase_C PF00544.14 Plants This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of Plants tissue.
Pentapeptide PF00805.17 Animals These repeats are found in many cyanobacterial proteins. The repeats were first identified in hglK. The function of these repeats is unknown. The structure of this repeat has been predicted to be a beta-helix. The repeat can be approximately described as A(D/N)LXX, where X can be any amino acid.
Pentapeptide_4 PF13599.1 Animals Unknown
Peptidase_C48 PF02902.14 Plants This domain contains the catalytic triad Cys-His-Asn.
Peptidase_C58 PF03543.9 All Unknown
Peptidase_C70 PF12385.3 Plants This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in Plants-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.
Peptidase_M85 PF13678.1 Animals This family of bacterial metallo-peptidases is thought to compromise the inflammatory response by degrading p65 thereby down-regulating the NF-kappaB signalling pathway. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52; and the heterodimeric p65-p50 complex appears to be most abundant one.
Peptidase_M91 PF14891.1 All This family of proteins contains an HEXXH motif, typical of zinc metallopeptidases. The family includes the E. coli effector protein NleD, which cleaves and inactivates c-Jun N-terminal kinase (JNK).
Pfam-B_11134 PB011134 Animals Unknown
Pfam-B_11530 PB011530 Plants Unknown
Pfam-B_12416 PB012416 Animals Unknown
Pfam-B_12597 PB012597 Animals Unknown
Pfam-B_13194 PB013194 Plants Unknown
Pfam-B_1373 PB001373 Animals Unknown
Pfam-B_14189 PB014189 Plants Unknown
Pfam-B_14193 PB014193 Animals Unknown
Pfam-B_14377 PB014377 Animals Unknown
Pfam-B_14881 PB014881 Animals Unknown
Pfam-B_15087 PB015087 Plants Unknown
Pfam-B_15534 PB015534 Animals Unknown
Pfam-B_1565 PB001565 Plants Unknown
Pfam-B_1580 PB001580 Plants Unknown
Pfam-B_15947 PB015947 Plants Unknown
Pfam-B_16213 PB016213 Plants Unknown
Pfam-B_16565 PB016565 Animals Unknown
Pfam-B_17109 PB017109 Animals Unknown
Pfam-B_19782 PB019782 Plants Unknown
Pfam-B_2365 PB002365 Animals Unknown
Pfam-B_2441 PB002441 Plants Unknown
Pfam-B_2762 PB002762 Plants Unknown
Pfam-B_278 PB000278 Animals Unknown
Pfam-B_2837 PB002837 Animals Unknown
Pfam-B_3148 PB003148 Plants Unknown
Pfam-B_3385 PB003385 Plants Unknown
Pfam-B_3415 PB003415 Animals Unknown
Pfam-B_373 PB000373 Animals Unknown
Pfam-B_4441 PB004441 Animals Unknown
Pfam-B_4505 PB004505 Plants Unknown
Pfam-B_4850 PB004850 Plants Unknown
Pfam-B_4943 PB004943 Animals Unknown
Pfam-B_5331 PB005331 Plants Unknown
Pfam-B_5480 PB005480 Animals Unknown
Pfam-B_5621 PB005621 Animals Unknown
Pfam-B_5638 PB005638 Plants Unknown
Pfam-B_5666 PB005666 Animals Unknown
Pfam-B_5781 PB005781 Plants Unknown
Pfam-B_5948 PB005948 Animals Unknown
Pfam-B_6188 PB006188 Animals Unknown
Pfam-B_6225 PB006225 Animals Unknown
Pfam-B_6230 PB006230 Animals Unknown
Pfam-B_6362 PB006362 Animals Unknown
Pfam-B_6720 PB006720 Animals Unknown
Pfam-B_7281 PB007281 Plants Unknown
Pfam-B_8638 PB008638 Animals Unknown
Pfam-B_9706 PB009706 Plants Unknown
PG_binding_1 PF01471.13 Plants This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
PipA PF07108.6 Animals This family consists of several Salmonella PipA (pathogenicity island-encoded protein A) and related phage sequences. PipA is thought to contribute to enteric but not to systemic salmonellosis. The family carries a highly conserved HEXXH sequence motif along with several highly conserved glutamic acid residues which might be indicative of the family being a metallo-peptidase.
Pkinase PF00069.20 Animals Unknown
PMT_C PF11647.3 Plants This family represents the C terminal region of Pasteurella multocida toxin (PMT) which displays a Trojan horse-like shape with three domains, C1, C2 and C3. The C3 domain possesses the Cys-His-Asp catalytic triad. PMT is an enzyme toxin carrying the cysteine protease-like catalytic triad which functions on the cytoplasmic face of the plasma membrane of target cells.
PTPlike_phytase PF14566.1 Plants Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organism Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteristic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.
Rac1 PF09632.5 Animals The Rac1-binding domain is the C-terminal portion of YpkA from Yersinia. It is an all-helical molecule consisting of two distinct subdomains connected by a linker. the N-terminal end, residues 434-615, consists of six helices organised into two three-helix bundles packed against each other. This region is involved with binding to GTPases. The C-terminal end, residues 705-732. is a novel and elongated fold consisting of four helices clustered into two pairs, and this fold carries the helix implicated in actin activation. Rac1-binding domain mimics host guanidine nucleotide dissociation inhibitors (GDIs) of the Rho GTPases, thereby inhibiting nucleotide exchange in Rac1 and causing cytoskeletal disruption in the host.
rve PF00665.21 Animals Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain PF02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain PF00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyses the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.
SecIII_SopE_N PF05364.9 Animals Salmonella typhimurium employs a type III secretion system to inject bacterial toxins into the host cell cytosol. These toxins transiently activate Rho family GTP-binding protein-dependent signaling cascades to induce cytoskeletal rearrangements. SopE, one of these toxins, can activate Cdc42 in a Dbl-like fashion via its C-terminal GEP domain PF07487. This family represents the N-terminal region of SopE. The function of this domain is unknown.
Shigella_OspC PF06128.6 Animals This family consists of the Shigella flexneri specific protein OspC. The function of this family is unknown but it is thought that Osp proteins may be involved in post invasion events related to virulence. Since bacterial pathogens adapt to multiple environments during the course of infecting a host, it has been proposed that Shigella evolved a mechanism to take advantage of a unique intracellular cue, which is mediated through MxiE, to express proteins when the organism reaches the eukaryotic cytosol.
SicP-binding PF09119.5 Animals Members of this family bind the chaperone SicP, which is required both to maintain the stability of SptP, as well as to ensure the eventual secretion of the protein. The domain is found in the Salmonella effector protein SptP, which interacts with SicP chaperone dimers mainly through four regions of its chaperone-binding domain. The structure of the SptP-SicP complex contains four molecules of SicP, aligned in a linear fashion and arranged in two sets of tightly bound homodimers that bind two SptP molecules. The SicP homodimers do not interact with each other, but are held together by a molecular interface formed between two SptP molecules. Each SptP molecule is wrapped around by three SicP chaperones (two chaperones from one homodimer and a third one from the opposite homodimer pair).
Sif PF06767.6 Animals This family consists of several SifA and SifB and SseJ proteins which seem to be specific to the Salmonella species. SifA, SifB and SseJ have been demonstrated to localise to the Salmonella-containing vacuole (SCV) and to Salmonella-induced filaments (Sifs). Trafficking of SseJ and SifB away from the SCV requires the SPI-2 effector SifA. SseJ trafficking away from the SCV along Sifs is unnecessary for its virulence function.
SipA PF09052.5 Animals Salmonella invasion protein A is an actin-binding protein that contributes to host cytoskeletal rearrangements by stimulating actin polymerisation and counteracting F-actin destabilising proteins. Members of this family possess an all-helical fold consisting of eight alpha-helices arranged so that six long, amphipathic helices form a compact fold that surrounds a final, predominantly hydrophobic helix in the middle of the molecule.
SLT PF01464.15 Plants This family is distantly related to PF00062. Members are found in phages, type II, type III and type IV secretion systems.
SLT_2 PF13406.1 Plants This family is related to the SLT domain
SopA_C PF13979.1 Animals This domain is found in the E. coli Type III secretion effector proteins SopA and NleL. These proteins have been shown to act as E3 ubiquitin ligase enzymes. This domain contains the active site cysteine residue.
SopD PF11047.3 Animals SopD is a type III virulence effector protein whose structure consists of 38% alpha-helix and 26% beta-strand.
SopE_GEF PF07487.8 Animals This family represents the C-terminal guanine nucleotide exchange factor (GEF) domain of SopE. Salmonella typhimurium employs a type III secretion system to inject bacterial toxins into the host cell cytosol. These toxins transiently activate Rho family GTP-binding protein-dependent signaling cascades to induce cytoskeletal rearrangements. SopE, can activate Cdc42, an essential component of the host cellular signaling cascade, in a Dbl-like fashion despite its lack of sequence similarity to Dbl-like proteins, the Rho-specific eukaryotic guanine nucleotide exchange factors.
SPAN PF02510.9 Animals Surface presentation of antigens protein (SPAN), also know as invasion protein invJ, is a Salmonella secretory pathway protein involved in presentation of determinants required for mammalian host cell invasion.
SpoA PF01052.15 Animals This family includes the C-terminal region of flagellar motor switch proteins FliN and FliM. It is associated with family FliM, PF02154.
SpvB PF03534.8 Animals Unknown
SseC PF04888.7 Animals SseC is a secreted protein that forms a complex together with SecB and SecD on the surface of Salmonella. All these proteins are secreted by the type III secretion system. Many mucosal pathogens use type III secretion systems for the injection of effector proteins into target cells. SecB, SseC and SecD are inserted into the target cell membrane. where they form a small pore or translocon. In addition to SseC, this family includes the bacterial secreted proteins PopB, PepB, YopB and EspD which are thought to be directly involved in pore formation, and type III secretion system translocon.
Tir_receptor_C PF07489.6 Animals Intimin and its translocated intimin receptor (Tir) are bacterial proteins that mediate adhesion between mammalian cells and attaching and effacing (A/E) pathogens. A unique and essential feature of A/E bacterial pathogens is the formation of actin-rich pedestals beneath the intimately adherent bacteria and localised destruction of the intestinal brush border. The bacterial outer membrane adhesin, intimin, is necessary for the production of the A/E lesion and diarrhoea. The A/E bacteria translocate their own receptor for intimin, Tir, into the membrane of mammalian cells using the type III secretion system. The translocated Tir triggers additional host signalling events and actin nucleation, which are essential for lesion formation. This family represents the Tir C-terminal domain which has been reported to bind uninfected host cells and beta-1 integrins although the role of intimin binding to integrins is unclear. This intimin C-terminal domain has also been shown to be sufficient for Tir recognition.
Tir_receptor_M PF03549.9 Animals Intimin and its translocated intimin receptor (Tir) are bacterial proteins that mediate adhesion between mammalian cells and attaching and effacing (A/E) pathogens. A unique and essential feature of A/E bacterial pathogens is the formation of actin-rich pedestals beneath the intimately adherent bacteria and localised destruction of the intestinal brush border. The bacterial outer membrane adhesin, intimin, is necessary for the production of the A/E lesion and diarrhoea. The A/E bacteria translocate their own receptor for intimin, Tir, into the membrane of mammalian cells using the type III secretion system. The translocated Tir triggers additional host signalling events and actin nucleation, which are essential for lesion formation. This family represents the Tir intimin-binding domain (Tir IBD) which is needed to bind intimin and support the predicted topology for Tir, with both N- and C-terminal regions in the mammalian cell cytosol.
Tir_receptor_N PF07490.6 Animals Intimin and its translocated intimin receptor (Tir) are bacterial proteins that mediate adhesion between mammalian cells and attaching and effacing (A/E) pathogens. A unique and essential feature of A/E bacterial pathogens is the formation of actin-rich pedestals beneath the intimately adherent bacteria and localised destruction of the intestinal brush border. The bacterial outer membrane adhesin, intimin, is necessary for the production of the A/E lesion and diarrhoea. The A/E bacteria translocate their own receptor for intimin, Tir, into the membrane of mammalian cells using the type III secretion system. The translocated Tir triggers additional host signalling events and actin nucleation, which are essential for lesion formation. This family represents the Tir N-terminal domain which is involved in Tir stability and Tir secretion.
Tox-PLDMTX PF15645.1 Animals A papain fold toxin domain found in bacterial polymorphic toxin systems.
Toxin_15 PF07906.8 Animals The members of this family are are sequences that are similar to the N-terminal half of the ShET2 enterotoxin produced by Shigella flexneri (Q47635) and Escherichia coli (Q47634). This protein was found to confer toxigenicity in the Ussing chamber, and the N-terminal region was found to be important for the protein's enterotoxic effect. It is thought to be a hydrophobic protein that forms inclusion bodies within the bacterial cell, and may be secreted by the Mxi system. Most members of this family are annotated as putative enterotoxins, but one member (Q8X606) is a regulator of acetyl CoA synthetase, and another two members (P76205 and P23325) are annotated as ankyrin-like regulatory proteins and contain Ank repeats (PF00023).
TTSSLRR PF12468.3 Animals This domain family is found in bacteria, and is approximately 50 amino acids in length. There are two completely conserved residues (Y and W) that may be functionally important. This family consists of leucine-rich repeat proteins involved in type III secretion.
TyeA PF09059.5 Animals Members of this family are composed of two pairs of parallel alpha-helices, and interact with the bacterial protein YopN via hydrophobic residues located on the helices. Association of TyeA with the C terminus of YopN is accompanied by conformational changes in both polypeptides that create order out of disorder: the resulting structure then serves as an impediment to type III secretion of YopN.
UPF0158 PF03682.8 Animals Unknown
Virul_Fac PF10139.4 Plants Members of this family of prokaryotic proteins include various putative virulence factor effector proteins. Their exact function is, as yet, unknown.
VRP3 PF03536.10 All Unknown
YopE PF03545.8 Animals Unknown
YopE_N PF09020.5 Animals The N terminal YopE domain targets YopE for secretion from the bacterium and translocation into eukaryotic cells.
YopH_N PF09013.5 Animals The N-terminal domain of YopH is a compact structure composed of four alpha-helices and two beta-hairpins. Helices alpha-1 and alpha-3 are parallel to each other and antiparallel to helices alpha-2 and alpha-4. This domain targets YopH for secretion from the bacterium and translocation into eukaryotic cells, and has phosphotyrosyl peptide-binding activity, allowing for recognition of p130Cas and paxillin.
YopJ PF03421.11 All The Yersinia effector YopJ inhibits the innate immune response by blocking MAP kinase and NFkappaB signaling pathways. YopJ is a serine/threonine acetyltransferase which regulates signalling pathways by blocking phosphorylation. Specifically, YopJ has been shown to block phosphorylation of active site residues. It has also been shown that YopJ acetyltransferase is activated by eukaryotic host cell inositol hexakisphosphate. This family was previously incorrectly annotated in Pfam as being a peptidase family.
YopR_core PF09025.5 Animals The YopR core domain, predominantly found in the Yersinia pestis virulence factor YopR, is composed of five alpha-helices, four of which are arranged in an antiparallel bundle. Little is known about this domain, though it may contribute to the virulence of the protein YopR.
Y_phosphatase PF00102.22 Animals Unknown