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Conserved domains on  [gi|487399824|ref|WP_001669236|]
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MULTISPECIES: CesT family type III secretion system chaperone [Salmonella]

Protein Classification

CesT family type III secretion system chaperone( domain architecture ID 13017812)

CesT family type III secretion system chaperone similar to Tir chaperone, which in Escherichia coli serves a chaperone function for translocated intimin receptor (Tir) protein; also similar to other chaperones such as sicP and Dspf

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T3SC_IA_CesT-like cd17023
Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT; This ...
 3-134 1.37e-67

Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT; This family includes type III secretion system (T3SS) chaperone proteins similar to Escherichia coli CesT and also contains Stm2138, a novel virulence chaperone in Salmonella enterica subsp. enterica serovar Typhimurium. In E. coli, the T3SS allows injection of the effector Tir (translocated intimin receptor), which plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions, and intracellular signal transduction. CesT binds to Tir, which interacts with intimin and anchors the infected cell membrane inside the host cytoplasm for signaling.


:

Pssm-ID: 409307  Cd Length: 133  Bit Score: 200.38  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824   3 SRADRLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGK-PPDNNNLAFEFLNANLWFAENNGP 81
Cdd:cd17023    1 SRSELLLKQFGEKIGIRSISFDENRLCSFAIDNDYYIILNDVNDEYLMIYGVCGKfPTDNSNLAFELLNANLWFAENNGP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487399824  82 HLCYDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENLYHILQDKGITLD 134
Cdd:cd17023   81 YLCYEPGAQSLLLALRFPLDEATPEKLENEIEVVLKSMENLYLILQEKGITLD 133
 
Name Accession Description Interval E-value
T3SC_IA_CesT-like cd17023
Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT; This ...
 3-134 1.37e-67

Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT; This family includes type III secretion system (T3SS) chaperone proteins similar to Escherichia coli CesT and also contains Stm2138, a novel virulence chaperone in Salmonella enterica subsp. enterica serovar Typhimurium. In E. coli, the T3SS allows injection of the effector Tir (translocated intimin receptor), which plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions, and intracellular signal transduction. CesT binds to Tir, which interacts with intimin and anchors the infected cell membrane inside the host cytoplasm for signaling.


Pssm-ID: 409307  Cd Length: 133  Bit Score: 200.38  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824   3 SRADRLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGK-PPDNNNLAFEFLNANLWFAENNGP 81
Cdd:cd17023    1 SRSELLLKQFGEKIGIRSISFDENRLCSFAIDNDYYIILNDVNDEYLMIYGVCGKfPTDNSNLAFELLNANLWFAENNGP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487399824  82 HLCYDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENLYHILQDKGITLD 134
Cdd:cd17023   81 YLCYEPGAQSLLLALRFPLDEATPEKLENEIEVVLKSMENLYLILQEKGITLD 133
CesT pfam05932
Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences ...
 7-122 6.58e-32

Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences which are highly similar to the Tir chaperone protein in E. Coli. In many Gram-negative bacteria, a key indicator of pathogenic potential is the possession of a specialized type III secretion system, which is utilized to deliver virulence effector proteins directly into the host cell cytosol. Many of the proteins secreted from such systems require small cytosolic chaperones to maintain the secreted substrates in a secretion-competent state. CesT serves a chaperone function for the enteropathogenic Escherichia coli (EPEC) translocated intimin receptor (Tir) protein, which confers upon EPEC the ability to alter host cell morphology following intimate bacterial attachment. This family also contains several DspF and related sequences from several plant pathogenic bacteria. The "disease-specific" (dsp) region next to the hrp gene cluster of Erwinia amylovora is required for pathogenicity but not for elicitation of the hypersensitive reaction. DspF and AvrF are small (16 kDa and 14 kDa) and acidic with predicted amphipathic alpha helices in their C termini; they resemble chaperones for virulence factors secreted by type III secretion systems of animal pathogens.


Pssm-ID: 399138  Cd Length: 119  Bit Score: 109.70  E-value: 6.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824    7 RLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGKPPDNN--NLAFEFLNANLWFAENNGPHLC 84
Cdd:pfam05932   1 QLLKEFARRLGLPPLVLDENGVCSLQIDDDVLILLLEHDSDELLLSTPLGDLPPDNdgRLLERLLEANLFGARTGGGALG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 487399824   85 YDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENL 122
Cdd:pfam05932  81 LDPKSGLLLLWARLPLESLDPAALEAALENLVALAERL 118
 
Name Accession Description Interval E-value
T3SC_IA_CesT-like cd17023
Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT; This ...
 3-134 1.37e-67

Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT; This family includes type III secretion system (T3SS) chaperone proteins similar to Escherichia coli CesT and also contains Stm2138, a novel virulence chaperone in Salmonella enterica subsp. enterica serovar Typhimurium. In E. coli, the T3SS allows injection of the effector Tir (translocated intimin receptor), which plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions, and intracellular signal transduction. CesT binds to Tir, which interacts with intimin and anchors the infected cell membrane inside the host cytoplasm for signaling.


Pssm-ID: 409307  Cd Length: 133  Bit Score: 200.38  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824   3 SRADRLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGK-PPDNNNLAFEFLNANLWFAENNGP 81
Cdd:cd17023    1 SRSELLLKQFGEKIGIRSISFDENRLCSFAIDNDYYIILNDVNDEYLMIYGVCGKfPTDNSNLAFELLNANLWFAENNGP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487399824  82 HLCYDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENLYHILQDKGITLD 134
Cdd:cd17023   81 YLCYEPGAQSLLLALRFPLDEATPEKLENEIEVVLKSMENLYLILQEKGITLD 133
CesT pfam05932
Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences ...
 7-122 6.58e-32

Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences which are highly similar to the Tir chaperone protein in E. Coli. In many Gram-negative bacteria, a key indicator of pathogenic potential is the possession of a specialized type III secretion system, which is utilized to deliver virulence effector proteins directly into the host cell cytosol. Many of the proteins secreted from such systems require small cytosolic chaperones to maintain the secreted substrates in a secretion-competent state. CesT serves a chaperone function for the enteropathogenic Escherichia coli (EPEC) translocated intimin receptor (Tir) protein, which confers upon EPEC the ability to alter host cell morphology following intimate bacterial attachment. This family also contains several DspF and related sequences from several plant pathogenic bacteria. The "disease-specific" (dsp) region next to the hrp gene cluster of Erwinia amylovora is required for pathogenicity but not for elicitation of the hypersensitive reaction. DspF and AvrF are small (16 kDa and 14 kDa) and acidic with predicted amphipathic alpha helices in their C termini; they resemble chaperones for virulence factors secreted by type III secretion systems of animal pathogens.


Pssm-ID: 399138  Cd Length: 119  Bit Score: 109.70  E-value: 6.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824    7 RLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGKPPDNN--NLAFEFLNANLWFAENNGPHLC 84
Cdd:pfam05932   1 QLLKEFARRLGLPPLVLDENGVCSLQIDDDVLILLLEHDSDELLLSTPLGDLPPDNdgRLLERLLEANLFGARTGGGALG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 487399824   85 YDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENL 122
Cdd:pfam05932  81 LDPKSGLLLLWARLPLESLDPAALEAALENLVALAERL 118
T3SC_I-like cd16364
class I type III secretion system (T3SS) chaperones and similar proteins; This family contains ...
 8-122 9.07e-14

class I type III secretion system (T3SS) chaperones and similar proteins; This family contains class I type III secretion system (T3SS) chaperones mainly found in Gram-negative bacteria such as Pseudomonas, Yersinia, Salmonella, Escherichia and Erwinia, among others. A wide variety of these bacterial pathogens and symbionts require a T3SS to inject eukaryotic host cells with effector proteins important for suppressing host defenses and establishing infection. Many of these effector proteins interact with specific type III secretion chaperones prior to secretion. These T3SS chaperones have been classified as class I type III secretion chaperones (T3SC), which are small structurally conserved dimers that interact specifically with T3SS effector proteins. Class I T3SC consists of two subclasses: IA and IB. Class IA T3SC binds a single effector, whereas class IB T3SC binds to several effectors. Class IA and Class IB T3SCs typically exhibit little sequence similarities, but share a common overall heart-shaped structure fold (alpha-beta-beta-beta-alpha-beta-beta-alpha) and features, such as a small size, an acidic pI and an amphipathic C-terminal alpha-helix. Chaperone protein CesT serves a chaperone function for the enteropathogenic Escherichia coli (EPEC) translocated intimin receptor (Tir) protein, which confers upon EPEC the ability to alter host cell morphology following intimate bacterial attachment. In Pseudomonas aeruginosa, chaperone ExsC binds small secreted protein ExsE as well as the non-secreted anti-activator protein ExsD; it relieves repression of the transcriptional activator ExsA (which activates expression of T3SS genes) by ExsD. P. aeruginosa SpcU binds the cytotoxin ExoU, which is a broad-specificity phospholipase A2 (PLA2) and lysophospholipase, and maintains the N-terminus of ExoU in an unfolded state which is required for secretion. Salmonella enterica chaperone SicP forms a complex with effector protein SptP at an early stage of its secretion process in order to avoid premature degradation, while chaperone SigE binds to effector SigD, which, upon translocation into the host cell, preferentially dephosphorylates specific inositol phospholipids that are thought to be crucial for subsequent activation of the host cell Ser-Thr kinase Akt. This family also includes Yersinia chaperone/escortee pairs SycE/YopE, SycH/YopH, SycT/YopT and SycN+YscB/YopN, all of which bind to specific Yersinia outer proteins (Yops). Also included are several DspF and related sequences from several plant pathogenic bacteria. The "disease-specific" (dsp) region next to the hrp gene cluster of Erwinia amylovora is required for pathogenicity but not for elicitation of the hypersensitive reaction. In addition, a group of proteins including Escherichia coli YbjN, Erwinia amylovora AmyR, and their homologs, are included in this family. They share a class I T3SC-like fold with T3SS chaperone proteins but appear to function independently of the T3SS.


Pssm-ID: 409301  Cd Length: 117  Bit Score: 63.18  E-value: 9.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824   8 LLRQFSLKLNTDSIVFDENRLCSFIIDnRYRILLT-STNSEYIMIYGFCGKPPDNNNLAF--EFLNANLWFAENNGPHLC 84
Cdd:cd16364    1 LLAELGQELGLPLLALDEDGVCSLTFD-GDEVTIElEEDDDRLLLYAVLGPLPPDDREALllLLLEANLFGQGTGGATLG 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 487399824  85 YDNNSQSLLLALNFSLNESSVEKLECEIEVVIRSMENL 122
Cdd:cd16364   80 LDPDTGELVLSRRLPLAGLDAEELEAALERFVEAAEAW 117
T3SC_IA_ShcA-like cd17019
Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae ...
 6-112 5.74e-11

Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae chaperone protein ShcA; This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas syringae ShcA and similar proteins. In P. syringae, which is a plant pathogen that can infect a wide range of species, the T3SS allows injection of the effector HopA1 (previously known as HopPsyA or HrmA), a protein that has unknown functions in the host cell but possesses close homologs that trigger the plant hypersensitive response in resistant strains. Chaperone ShcA binding to Hop1A shows that interactions in animal pathogens are preserved in the Gram-negative pathogens of plants.


Pssm-ID: 409303  Cd Length: 122  Bit Score: 55.71  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824   6 DRLLRQFSLKLNTDSIVFDENRLCSFIIDNRYRILLTSTNSEYIMIYGFCGKPPD---NNNLAFEFLNANLWFAENNGPH 82
Cdd:cd17019    2 DRLLAEFASQLGIPPLSFDEDGLCQLLIDEDLAIALRRDEAERLTLIGELDDPLPdalDDDLLRLLLEAALNPLRGDGPG 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 487399824  83 LCYDNNSQSLLLALNFSLNESSVEKLECEI 112
Cdd:cd17019   82 IGWHPESGGLIAYRHLPLTKLSAERLSEEL 111
T3SC_IA_SicP-like cd17021
Class IA type III secretion system chaperone protein, similar to Salmonella enterica chaperone ...
 6-126 2.92e-05

Class IA type III secretion system chaperone protein, similar to Salmonella enterica chaperone protein SicP; This family includes type III secretion system (T3SS) chaperone proteins similar to Salmonella enterica SicP and similar proteins. In S. enterica, many of its serovars being serious human pathogens, the T3SS allows injection of the effector SptP, a virulence protein that is involved in bacterial invasion into a host cell. Chaperone SicP forms a complex with SptP at an early stage of the effector protein secretion process in order to avoid premature degradation; also, the complex is dissociated at a late stage to secrete only SptP with the help of the ATPase InvC which is part of the related T3SS injectisome.


Pssm-ID: 409305  Cd Length: 121  Bit Score: 40.69  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487399824   6 DRLLRQFSLKLNTDsIVFDENRLCSFIIDNRYRILLtSTNSEYIMIYGF-CGKPPDNNNLAFEF-LNANLWFAENNGPHL 83
Cdd:cd17021    2 EKILAELGQKLGIP-LLLDENGQCTLLLDDGLFISI-RANDDRWYLYAMlATLPDGDDNALWKKiLELNLSLAETGGGVL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 487399824  84 CYDNNSQSLLLALNFSlNESSVEKLECEIEVVIRSMENLYHIL 126
Cdd:cd17021   80 GYSESADALLYLLRIP-VPLNLDALEAQLERFVNQVEALRQEL 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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