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Conserved domains on  [gi|488158586|ref|WP_002229794|]
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MULTISPECIES: type III secretion chaperone SycN [Yersinia pseudotuberculosis complex]

Protein Classification

type III secretion chaperone SycN( domain architecture ID 10020797)

type III secretion chaperone SycN 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_SycN TIGR02503
type III secretion chaperone SycN; Members of this protein family are part of the machinery of ...
 4-122 6.32e-46

type III secretion chaperone SycN; Members of this protein family are part of the machinery of bacterial type III secretion in a number of bacteria that target animal cells. In the well-studied system from Yersinia, a complex of this protein (SycN) and YscB (pfam07329) acts as a chaperone for the export of YopN (). YopN then acts to control effector protein secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell. [Protein fate, Protein folding and stabilization, Cellular processes, Pathogenesis]


:

Pssm-ID: 131555  Cd Length: 119  Bit Score: 144.53  E-value: 6.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488158586    4 IEPIISHFCQDLGVPTSSPLSPLIQLEMAQSGTLQLEQHGATLTLWLARSLAWHRCEDAMVKALTLTAAQKSGALPLRAG 83
Cdd:TIGR02503   1 IDRALAQFCQDLGLPTPAPLPRLAQLSMEQSGRLYVEQHDGTLLLWLARSLEWHQAEEALKRALTLCHAQRGGALPLRAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 488158586   84 WLGESQLVLFVSLDERSLTLPLLHQAFEQLLRLQQEVLA 122
Cdd:TIGR02503  81 LLGEQQLVLCTRLDGRSLTAPTLHQAFVQLLRLLDEVTA 119
 
Name Accession Description Interval E-value
type_III_SycN TIGR02503
type III secretion chaperone SycN; Members of this protein family are part of the machinery of ...
 4-122 6.32e-46

type III secretion chaperone SycN; Members of this protein family are part of the machinery of bacterial type III secretion in a number of bacteria that target animal cells. In the well-studied system from Yersinia, a complex of this protein (SycN) and YscB (pfam07329) acts as a chaperone for the export of YopN (). YopN then acts to control effector protein secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell. [Protein fate, Protein folding and stabilization, Cellular processes, Pathogenesis]


Pssm-ID: 131555  Cd Length: 119  Bit Score: 144.53  E-value: 6.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488158586    4 IEPIISHFCQDLGVPTSSPLSPLIQLEMAQSGTLQLEQHGATLTLWLARSLAWHRCEDAMVKALTLTAAQKSGALPLRAG 83
Cdd:TIGR02503   1 IDRALAQFCQDLGLPTPAPLPRLAQLSMEQSGRLYVEQHDGTLLLWLARSLEWHQAEEALKRALTLCHAQRGGALPLRAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 488158586   84 WLGESQLVLFVSLDERSLTLPLLHQAFEQLLRLQQEVLA 122
Cdd:TIGR02503  81 LLGEQQLVLCTRLDGRSLTAPTLHQAFVQLLRLLDEVTA 119
T3SC_IA_SycN-like cd17031
Class IA type III secretion system chaperone protein, similar to Yersinia pestis SycN; This ...
 4-120 5.05e-41

Class IA type III secretion system chaperone protein, similar to Yersinia pestis SycN; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis SycN and similar proteins. In Yersinia pestis, the causative agent of bubonic and pneumonic 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 and have been linked to cytolysis. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex; SycN-YscB forms a heterodimeric secretion chaperone and binds YopN, a key part of a complex that regulates type III secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell. Negative regulation is mediated by the complex by blocking the entrance to the secretion apparatus prior to contact with mammalian cells.


Pssm-ID: 409315  Cd Length: 118  Bit Score: 131.97  E-value: 5.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488158586   4 IEPIISHFCQDLGVPTSSP-LSPLIQLEMAQSGTLQLEQHGATLTLWLARSLAWHRCEDAMVKALTLTAAQKSGALPLRA 82
Cdd:cd17031    1 IDDAIAEFGRSMGVPGLELsGSGIIALEFERGGTLFLERQGDGLLLYLAREIPEHHDAEAAAKALRLCHYDQSLPFPVQA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488158586  83 GWLGESQLVLFVSLDERSLTLPLLHQAFEQLLRLQQEV 120
Cdd:cd17031   81 GLLGDNQLVLLARLDEREVTLPTLEQALQLLTRLHDEV 118
 
Name Accession Description Interval E-value
type_III_SycN TIGR02503
type III secretion chaperone SycN; Members of this protein family are part of the machinery of ...
 4-122 6.32e-46

type III secretion chaperone SycN; Members of this protein family are part of the machinery of bacterial type III secretion in a number of bacteria that target animal cells. In the well-studied system from Yersinia, a complex of this protein (SycN) and YscB (pfam07329) acts as a chaperone for the export of YopN (). YopN then acts to control effector protein secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell. [Protein fate, Protein folding and stabilization, Cellular processes, Pathogenesis]


Pssm-ID: 131555  Cd Length: 119  Bit Score: 144.53  E-value: 6.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488158586    4 IEPIISHFCQDLGVPTSSPLSPLIQLEMAQSGTLQLEQHGATLTLWLARSLAWHRCEDAMVKALTLTAAQKSGALPLRAG 83
Cdd:TIGR02503   1 IDRALAQFCQDLGLPTPAPLPRLAQLSMEQSGRLYVEQHDGTLLLWLARSLEWHQAEEALKRALTLCHAQRGGALPLRAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 488158586   84 WLGESQLVLFVSLDERSLTLPLLHQAFEQLLRLQQEVLA 122
Cdd:TIGR02503  81 LLGEQQLVLCTRLDGRSLTAPTLHQAFVQLLRLLDEVTA 119
T3SC_IA_SycN-like cd17031
Class IA type III secretion system chaperone protein, similar to Yersinia pestis SycN; This ...
 4-120 5.05e-41

Class IA type III secretion system chaperone protein, similar to Yersinia pestis SycN; This family includes type III secretion system (T3SS) chaperone proteins similar to Yersinia pestis SycN and similar proteins. In Yersinia pestis, the causative agent of bubonic and pneumonic 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 and have been linked to cytolysis. The secretion of Yops is regulated by the activity of the YopN/SycN/YscB/TyeA complex; SycN-YscB forms a heterodimeric secretion chaperone and binds YopN, a key part of a complex that regulates type III secretion, in response to calcium levels, so that secretion occurs only after contact with the targeted eukaryotic cell. Negative regulation is mediated by the complex by blocking the entrance to the secretion apparatus prior to contact with mammalian cells.


Pssm-ID: 409315  Cd Length: 118  Bit Score: 131.97  E-value: 5.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488158586   4 IEPIISHFCQDLGVPTSSP-LSPLIQLEMAQSGTLQLEQHGATLTLWLARSLAWHRCEDAMVKALTLTAAQKSGALPLRA 82
Cdd:cd17031    1 IDDAIAEFGRSMGVPGLELsGSGIIALEFERGGTLFLERQGDGLLLYLAREIPEHHDAEAAAKALRLCHYDQSLPFPVQA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488158586  83 GWLGESQLVLFVSLDERSLTLPLLHQAFEQLLRLQQEV 120
Cdd:cd17031   81 GLLGDNQLVLLARLDEREVTLPTLEQALQLLTRLHDEV 118
 
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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