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Conserved domains on  [gi|916621815|ref|WP_051228906|]
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CesT family type III secretion system chaperone [Paludibacterium yongneupense]

Protein Classification

type III secretion system chaperone( domain architecture ID 13017821)

class I type III secretion system chaperone is required in the injection into host cells of effector proteins that are important for suppressing host defenses and establishing infection

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T3SC_IA_SycT-like cd17032
Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT; ...
 15-123 2.41e-61

Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia enterocolitica SycT and similar proteins. In Y. enterocolitica, a food-borne pathogen causing gastroenteritis and mesenteric lymphadenitis, chaperone SycT promotes translocation of effector YopT (Yersinia outer protein T), a cysteine protease that inactivates the small GTPase RhoA of targeted host cells by cleaving its C-terminal, prenylated cysteine, thereby releasing the GTPase into the host cytosol.


:

Pssm-ID: 409316  Cd Length: 121  Bit Score: 183.85  E-value: 2.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916621815  15 SGFAFDTCEETMVSLRCGDGLRVYLAAYQDRWLVLYHELDgdCGPVTPDNLFGRHWPAHVLSPVDGIWILWSQQPLAGLS 94
Cdd:cd17032   15 LGLNHQTNEDGIYTLEVDGHIQVLIACYHDQWLQLFSELG--SELPTNDNLFGEHWPAHVQGRLDGKAILWSQQPLAGLD 92

                         90       100
                 ....*....|....*....|....*....
gi 916621815  95 EHALECWVSDFAASVARYRSPAAATEKAR 123
Cdd:cd17032   93 VAELQAWLERFIDDIEQRKEPQNTKEPPN 121
 
Name Accession Description Interval E-value
T3SC_IA_SycT-like cd17032
Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT; ...
 15-123 2.41e-61

Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia enterocolitica SycT and similar proteins. In Y. enterocolitica, a food-borne pathogen causing gastroenteritis and mesenteric lymphadenitis, chaperone SycT promotes translocation of effector YopT (Yersinia outer protein T), a cysteine protease that inactivates the small GTPase RhoA of targeted host cells by cleaving its C-terminal, prenylated cysteine, thereby releasing the GTPase into the host cytosol.


Pssm-ID: 409316  Cd Length: 121  Bit Score: 183.85  E-value: 2.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916621815  15 SGFAFDTCEETMVSLRCGDGLRVYLAAYQDRWLVLYHELDgdCGPVTPDNLFGRHWPAHVLSPVDGIWILWSQQPLAGLS 94
Cdd:cd17032   15 LGLNHQTNEDGIYTLEVDGHIQVLIACYHDQWLQLFSELG--SELPTNDNLFGEHWPAHVQGRLDGKAILWSQQPLAGLD 92

                         90       100
                 ....*....|....*....|....*....
gi 916621815  95 EHALECWVSDFAASVARYRSPAAATEKAR 123
Cdd:cd17032   93 VAELQAWLERFIDDIEQRKEPQNTKEPPN 121
CesT pfam05932
Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences ...
 15-113 2.23e-08

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: 48.84  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916621815   15 SGFAFDtcEETMVSLRCGDGLRVYLAAYQDRWLVLYheldGDCGPVTPDN-------------LFGRHWPAHV-LSPVDG 80
Cdd:pfam05932  13 PPLVLD--ENGVCSLQIDDDVLILLLEHDSDELLLS----TPLGDLPPDNdgrllerlleanlFGARTGGGALgLDPKSG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 916621815   81 IWILWSQQPLAGLSEHALECWVSDFAASVARYR 113
Cdd:pfam05932  87 LLLLWARLPLESLDPAALEAALENLVALAERLR 119
 
Name Accession Description Interval E-value
T3SC_IA_SycT-like cd17032
Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT; ...
 15-123 2.41e-61

Class IA type III secretion system chaperone protein, similar to Yersinia enterocolitica SycT; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia enterocolitica SycT and similar proteins. In Y. enterocolitica, a food-borne pathogen causing gastroenteritis and mesenteric lymphadenitis, chaperone SycT promotes translocation of effector YopT (Yersinia outer protein T), a cysteine protease that inactivates the small GTPase RhoA of targeted host cells by cleaving its C-terminal, prenylated cysteine, thereby releasing the GTPase into the host cytosol.


Pssm-ID: 409316  Cd Length: 121  Bit Score: 183.85  E-value: 2.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916621815  15 SGFAFDTCEETMVSLRCGDGLRVYLAAYQDRWLVLYHELDgdCGPVTPDNLFGRHWPAHVLSPVDGIWILWSQQPLAGLS 94
Cdd:cd17032   15 LGLNHQTNEDGIYTLEVDGHIQVLIACYHDQWLQLFSELG--SELPTNDNLFGEHWPAHVQGRLDGKAILWSQQPLAGLD 92

                         90       100
                 ....*....|....*....|....*....
gi 916621815  95 EHALECWVSDFAASVARYRSPAAATEKAR 123
Cdd:cd17032   93 VAELQAWLERFIDDIEQRKEPQNTKEPPN 121
CesT pfam05932
Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences ...
 15-113 2.23e-08

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: 48.84  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916621815   15 SGFAFDtcEETMVSLRCGDGLRVYLAAYQDRWLVLYheldGDCGPVTPDN-------------LFGRHWPAHV-LSPVDG 80
Cdd:pfam05932  13 PPLVLD--ENGVCSLQIDDDVLILLLEHDSDELLLS----TPLGDLPPDNdgrllerlleanlFGARTGGGALgLDPKSG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 916621815   81 IWILWSQQPLAGLSEHALECWVSDFAASVARYR 113
Cdd:pfam05932  87 LLLLWARLPLESLDPAALEAALENLVALAERLR 119
T3SC_I-like cd16364
class I type III secretion system (T3SS) chaperones and similar proteins; This family contains ...
 32-111 2.27e-03

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: 35.44  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916621815  32 GDGLRVYLAAYQDRwLVLYHELdgdcGPVTPD------------NLFGRHWPAHVLS--PVDGIWILWSQQPLAGLSEHA 97
Cdd:cd16364   28 GDEVTIELEEDDDR-LLLYAVL----GPLPPDdrealllllleaNLFGQGTGGATLGldPDTGELVLSRRLPLAGLDAEE 102

                         90
                 ....*....|....
gi 916621815  98 LECWVSDFAASVAR 111
Cdd:cd16364  103 LEAALERFVEAAEA 116
T3SC_IA_ShcF-like cd17025
Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae ShcF; ...
 32-98 4.67e-03

Class IA type III secretion system chaperone protein, similar to Pseudomonas syringae ShcF; This family includes type III secretion system (T3SS) chaperone proteins similar to Pseudomonas syringae ShcF 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 protein AvrPphF into genetically susceptible host cells. Chaperone ShcF (originally known as AvrPphF ORD1) binds AvrPphF in a similar manner to type III chaperones from bacterial pathogens of animals, indicating structural conservation of these specialized chaperones, despite high sequence divergence.


Pssm-ID: 409309  Cd Length: 124  Bit Score: 34.56  E-value: 4.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 916621815  32 GDGLRVYLAAYQDRWLVLYHEL---DGDCGPVTPD-----NLFGRHWPAHVLS--PVDGIWILWSQQPLAGLSEHAL 98
Cdd:cd17025   31 DDGLSIHLLGNPRGYLTLSCLLgvpDERSDEELLLellqaNLFSLEHPPIIIGldAEQDKLVLWTRQPLAELDEAEL 107
 
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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