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Conserved domains on  [gi|488141717|ref|WP_002212925|]
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MULTISPECIES: type III secretion system chaperone YscB [Yersinia pseudotuberculosis complex]

Protein Classification

YscB family type III secretion system chaperone( domain architecture ID 10020802)

YscB family type III secretion system chaperone similar to chaperone protein YscB, which acts as a specific chaperone for YopN and may facilitate its secretion and subsequent translocation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type_III_yscB TIGR02513
type III secretion system chaperone, YscB family; Members of this family include YscB of ...
 2-137 1.20e-63

type III secretion system chaperone, YscB family; Members of this family include YscB of Yersinia and functionally equivalent (but differently named) proteins from type III secretion systems of other pathogens that affect animal cells. YscB acts, along with SycN (TIGR02503), as a chaperone for YopN, a key part of a complex that regulates type III secretion so it responds to contact with the eukaryotic target cell.


:

Pssm-ID: 131565  Cd Length: 139  Bit Score: 190.80  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717    2 QNLLKNLAASLGRKPFVADKQGVYRLTIDKHLVMLAPHGSELVLRTPIDAPMLREGNNVNVTLLRSLMQQALAWAKRYPQ 81
Cdd:TIGR02513   1 QNLLKNLAARLGQGPFVADRQGVYHLTIDQHLVMLAQHGSELVLETPLDARMLRPGDNQNVTLLRSLMQQVLAWARRYPQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488141717   82 TLVLDDCGQLVLEARLRLQELDTHGLQEVINKQLALLEHLIPQLTPFSV---ASRVGWN 137
Cdd:TIGR02513  81 ALVLDADGQLILEARLRLDELDTHGLEEVLAQQVALLEHLMPQLEPFSVnhtASRVVWN 139
 
Name Accession Description Interval E-value
type_III_yscB TIGR02513
type III secretion system chaperone, YscB family; Members of this family include YscB of ...
 2-137 1.20e-63

type III secretion system chaperone, YscB family; Members of this family include YscB of Yersinia and functionally equivalent (but differently named) proteins from type III secretion systems of other pathogens that affect animal cells. YscB acts, along with SycN (TIGR02503), as a chaperone for YopN, a key part of a complex that regulates type III secretion so it responds to contact with the eukaryotic target cell.


Pssm-ID: 131565  Cd Length: 139  Bit Score: 190.80  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717    2 QNLLKNLAASLGRKPFVADKQGVYRLTIDKHLVMLAPHGSELVLRTPIDAPMLREGNNVNVTLLRSLMQQALAWAKRYPQ 81
Cdd:TIGR02513   1 QNLLKNLAARLGQGPFVADRQGVYHLTIDQHLVMLAQHGSELVLETPLDARMLRPGDNQNVTLLRSLMQQVLAWARRYPQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488141717   82 TLVLDDCGQLVLEARLRLQELDTHGLQEVINKQLALLEHLIPQLTPFSV---ASRVGWN 137
Cdd:TIGR02513  81 ALVLDADGQLILEARLRLDELDTHGLEEVLAQQVALLEHLMPQLEPFSVnhtASRVVWN 139
T3SC_IA_YscB_AscB-like cd17027
Class IA type III secretion system chaperone protein, similar to Yersinia pestis YscB; This ...
 1-127 3.92e-35

Class IA type III secretion system chaperone protein, similar to Yersinia pestis YscB; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis YscB and its homologs, Aeromonas hydrophila AscB and Photorhabdus luminescens LscB. In Yersinia pestis, which causes the deadly bubonic plague, the T3SS allows injection of effector proteins, termed Yersinia outer proteins (Yops) into macrophages and other immune cells, forming pores in the host cell membrane. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex. YscB acts, along with SycN, as a chaperone for YopN, a key part of a complex that regulates type III secretion so that it responds to contact with the eukaryotic target cell.


Pssm-ID: 409311  Cd Length: 127  Bit Score: 117.75  E-value: 3.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717   1 MQNLLKNLAASLGRKPFVADKQGVYRLTIDKHL-VMLAPHGSELVLRTPIDAPMLREGnnVNVTLLRSLMQQALAWAKRY 79
Cdd:cd17027    1 LDNLLASLAARLGIGPLVADQDGRYTLRFDGRLeVRLFQAGGWLLLEAQLAALPTDDG--QREELLKKLLQKALALLRTQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488141717  80 PQTLVLD-DCGQLVLEARLRLQELDTHGLQEVINKQLALLEHLIPQLTP 127
Cdd:cd17027   79 RSSLSLDpDEDALLLYRRLALEGLSPDDFEEALEEFLNALERWREELGQ 127
CesT pfam05932
Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences ...
 3-121 8.55e-25

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: 91.21  E-value: 8.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717    3 NLLKNLAASLGRKPFVADKQGVYRLTIDK--HLVMLAPHGSELVLRTPIDAPMLREGNNvnvtLLRSLMQQALAWAKRYP 80
Cdd:pfam05932   1 QLLKEFARRLGLPPLVLDENGVCSLQIDDdvLILLLEHDSDELLLSTPLGDLPPDNDGR----LLERLLEANLFGARTGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488141717   81 QTLVLD-DCGQLVLEARLRLQELDTHGLQEVINKQLALLEHL 121
Cdd:pfam05932  77 GALGLDpKSGLLLLWARLPLESLDPAALEAALENLVALAERL 118
 
Name Accession Description Interval E-value
type_III_yscB TIGR02513
type III secretion system chaperone, YscB family; Members of this family include YscB of ...
 2-137 1.20e-63

type III secretion system chaperone, YscB family; Members of this family include YscB of Yersinia and functionally equivalent (but differently named) proteins from type III secretion systems of other pathogens that affect animal cells. YscB acts, along with SycN (TIGR02503), as a chaperone for YopN, a key part of a complex that regulates type III secretion so it responds to contact with the eukaryotic target cell.


Pssm-ID: 131565  Cd Length: 139  Bit Score: 190.80  E-value: 1.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717    2 QNLLKNLAASLGRKPFVADKQGVYRLTIDKHLVMLAPHGSELVLRTPIDAPMLREGNNVNVTLLRSLMQQALAWAKRYPQ 81
Cdd:TIGR02513   1 QNLLKNLAARLGQGPFVADRQGVYHLTIDQHLVMLAQHGSELVLETPLDARMLRPGDNQNVTLLRSLMQQVLAWARRYPQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488141717   82 TLVLDDCGQLVLEARLRLQELDTHGLQEVINKQLALLEHLIPQLTPFSV---ASRVGWN 137
Cdd:TIGR02513  81 ALVLDADGQLILEARLRLDELDTHGLEEVLAQQVALLEHLMPQLEPFSVnhtASRVVWN 139
T3SC_IA_YscB_AscB-like cd17027
Class IA type III secretion system chaperone protein, similar to Yersinia pestis YscB; This ...
 1-127 3.92e-35

Class IA type III secretion system chaperone protein, similar to Yersinia pestis YscB; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis YscB and its homologs, Aeromonas hydrophila AscB and Photorhabdus luminescens LscB. In Yersinia pestis, which causes the deadly bubonic plague, the T3SS allows injection of effector proteins, termed Yersinia outer proteins (Yops) into macrophages and other immune cells, forming pores in the host cell membrane. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex. YscB acts, along with SycN, as a chaperone for YopN, a key part of a complex that regulates type III secretion so that it responds to contact with the eukaryotic target cell.


Pssm-ID: 409311  Cd Length: 127  Bit Score: 117.75  E-value: 3.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717   1 MQNLLKNLAASLGRKPFVADKQGVYRLTIDKHL-VMLAPHGSELVLRTPIDAPMLREGnnVNVTLLRSLMQQALAWAKRY 79
Cdd:cd17027    1 LDNLLASLAARLGIGPLVADQDGRYTLRFDGRLeVRLFQAGGWLLLEAQLAALPTDDG--QREELLKKLLQKALALLRTQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488141717  80 PQTLVLD-DCGQLVLEARLRLQELDTHGLQEVINKQLALLEHLIPQLTP 127
Cdd:cd17027   79 RSSLSLDpDEDALLLYRRLALEGLSPDDFEEALEEFLNALERWREELGQ 127
CesT pfam05932
Tir chaperone protein (CesT) family; This family consists of a number of bacterial sequences ...
 3-121 8.55e-25

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: 91.21  E-value: 8.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717    3 NLLKNLAASLGRKPFVADKQGVYRLTIDK--HLVMLAPHGSELVLRTPIDAPMLREGNNvnvtLLRSLMQQALAWAKRYP 80
Cdd:pfam05932   1 QLLKEFARRLGLPPLVLDENGVCSLQIDDdvLILLLEHDSDELLLSTPLGDLPPDNDGR----LLERLLEANLFGARTGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488141717   81 QTLVLD-DCGQLVLEARLRLQELDTHGLQEVINKQLALLEHL 121
Cdd:pfam05932  77 GALGLDpKSGLLLLWARLPLESLDPAALEAALENLVALAERL 118
T3SC_I-like cd16364
class I type III secretion system (T3SS) chaperones and similar proteins; This family contains ...
 4-121 1.73e-09

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: 52.00  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141717   4 LLKNLAASLGRKPFVADKQGVYRLTIDKH--LVMLAPHGSELVLRTPIDAPMLREGNNvnvtLLRSLMQQALAWAKRYPQ 81
Cdd:cd16364    1 LLAELGQELGLPLLALDEDGVCSLTFDGDevTIELEEDDDRLLLYAVLGPLPPDDREA----LLLLLLEANLFGQGTGGA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488141717  82 TLVLD-DCGQLVLEARLRLQELDTHGLQEVINKQLALLEHL 121
Cdd:cd16364   77 TLGLDpDTGELVLSRRLPLAGLDAEELEAALERFVEAAEAW 117
 
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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