NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15833815|ref|NP_312588|]
View 

T3SS translocated intimin receptor Tir [Escherichia coli O157:H7 str. Sakai]

Protein Classification

type III secretion system LEE translocated intimin receptor Tir( domain architecture ID 10538717)

type III secretion system LEE translocated intimin receptor Tir is a multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection; contains an extracellular domain that acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Tir_receptor_N pfam07490
Translocated intimin receptor (Tir) N-terminus; Intimin and its translocated intimin receptor ...
 1-267 1.32e-150

Translocated intimin receptor (Tir) N-terminus; 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 localized 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.


:

Pssm-ID: 254231  Cd Length: 269  Bit Score: 432.84  E-value: 1.32e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815     1 MPIGNLGHNPNVNNSIPPAPPLPSQTDGA-GGRGQLINSTGPLGSRALFTPVRNSMADSGDNRASDVPGLPVNPMRLAAS 79
Cdd:pfam07490   1 MPIGNLGHNPNVNALIPPAPPLPSQTDGArGGRGQLISSTGALGSRLLFTPIRNSVADSVDSRASDIPGLPVNPLRLAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815    80 EITLNDGFEVLHDHGPLDTLNRQIGSSVFRVETQEDGKHIAVGQRNGVETSVVLSDQEYARLQSIDPEGKDKFVFTGGRG 159
Cdd:pfam07490  81 EITLNGGFEVLHDKGPLDTLNTQIGSSAFRVETQDDGSHVAIGQKNGLETSVVLSEQEFSSLQAIDPEGKNRFVFTGGRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   160 GAGHAMVTVASDITEARQRILELLEPKGTGESKGAGeskgvgelRESNSGAENTTETQTST---------STSSLRSDPK 230
Cdd:pfam07490 161 GAGHAMVTVASDIAEARQRILDKLEPKDTGGRQAKD--------RTSNSGGVNSAEGQDDGtssethtstSTSSLRSDPK 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 15833815   231 LWLALGTVATGLIGLAATGIVQALALTPEPDSPTTTD 267
Cdd:pfam07490 233 LWLSLGTIAAGLIGLAATGIAQALALTPEPDDPTTTD 269
Tir_receptor_C pfam07489
Translocated intimin receptor (Tir) C-terminus; Intimin and its translocated intimin receptor ...
 334-558 2.09e-96

Translocated intimin receptor (Tir) C-terminus; 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 localized 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.


:

Pssm-ID: 369388  Cd Length: 222  Bit Score: 292.69  E-value: 2.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   334 IENNAQAQKKYDEQQAKRQEELKVSSGAGYGLSGALILGGGIGVAVTAALHRKNQPVEQTTTTTTTTTTTSArTVENKPA 413
Cdd:pfam07489   1 IESNAQAQQRYDEQQAKRQEELNLSSGAGYGLSGALILGGGIGAGVTAALHRRNQPVEQTTTTTTTTTTTST-TVENKPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   414 NNTPAQGNVDTPGSEDTMESRRSSMASTSST-FFDTSSIGTVQNPYADVKTSLHDSQVptSNSNTSVQNMGNTDSVVYST 492
Cdd:pfam07489  80 NNTPAQGNTDTSGAEETASSRRSSQASTASTtWSDTSSIDTVQNPYADVGMSRNDSQA--RNPEEPIYDEVAADSPIYSV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833815   493 IQHPPRDTTDNGaRLLGNPSAGIQSTYARLALSGGLRHDMGGLTGGSNSAVNTSNNPPAPGSHRFV 558
Cdd:pfam07489 158 IQHFSGDTPDTG-RLLGNPGQGIQSTYALLASSGGLRLGMGGLTGGGESAVSTANAAPTPGSHRFV 222
Tir_receptor_M pfam03549
Translocated intimin receptor (Tir) intimin-binding domain; Intimin and its translocated ...
 269-333 1.19e-29

Translocated intimin receptor (Tir) intimin-binding domain; 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 localized 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.


:

Pssm-ID: 460968  Cd Length: 65  Bit Score: 111.02  E-value: 1.19e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833815   269 DAAASATETATRDQLTKEAFQNPDNQKVNIDELGNAIPSGVLKDDVVANIEEQAKAAGEEAKQQA 333
Cdd:pfam03549   1 DAAASAAETATKDQLTQEAFQNPDNQKVNIDENGNAIPSGELKDDVVAQIAEQAKAAGEEARQQA 65
 
Name Accession Description Interval E-value
Tir_receptor_N pfam07490
Translocated intimin receptor (Tir) N-terminus; Intimin and its translocated intimin receptor ...
 1-267 1.32e-150

Translocated intimin receptor (Tir) N-terminus; 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 localized 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.


Pssm-ID: 254231  Cd Length: 269  Bit Score: 432.84  E-value: 1.32e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815     1 MPIGNLGHNPNVNNSIPPAPPLPSQTDGA-GGRGQLINSTGPLGSRALFTPVRNSMADSGDNRASDVPGLPVNPMRLAAS 79
Cdd:pfam07490   1 MPIGNLGHNPNVNALIPPAPPLPSQTDGArGGRGQLISSTGALGSRLLFTPIRNSVADSVDSRASDIPGLPVNPLRLAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815    80 EITLNDGFEVLHDHGPLDTLNRQIGSSVFRVETQEDGKHIAVGQRNGVETSVVLSDQEYARLQSIDPEGKDKFVFTGGRG 159
Cdd:pfam07490  81 EITLNGGFEVLHDKGPLDTLNTQIGSSAFRVETQDDGSHVAIGQKNGLETSVVLSEQEFSSLQAIDPEGKNRFVFTGGRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   160 GAGHAMVTVASDITEARQRILELLEPKGTGESKGAGeskgvgelRESNSGAENTTETQTST---------STSSLRSDPK 230
Cdd:pfam07490 161 GAGHAMVTVASDIAEARQRILDKLEPKDTGGRQAKD--------RTSNSGGVNSAEGQDDGtssethtstSTSSLRSDPK 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 15833815   231 LWLALGTVATGLIGLAATGIVQALALTPEPDSPTTTD 267
Cdd:pfam07490 233 LWLSLGTIAAGLIGLAATGIAQALALTPEPDDPTTTD 269
Tir_receptor_C pfam07489
Translocated intimin receptor (Tir) C-terminus; Intimin and its translocated intimin receptor ...
 334-558 2.09e-96

Translocated intimin receptor (Tir) C-terminus; 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 localized 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.


Pssm-ID: 369388  Cd Length: 222  Bit Score: 292.69  E-value: 2.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   334 IENNAQAQKKYDEQQAKRQEELKVSSGAGYGLSGALILGGGIGVAVTAALHRKNQPVEQTTTTTTTTTTTSArTVENKPA 413
Cdd:pfam07489   1 IESNAQAQQRYDEQQAKRQEELNLSSGAGYGLSGALILGGGIGAGVTAALHRRNQPVEQTTTTTTTTTTTST-TVENKPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   414 NNTPAQGNVDTPGSEDTMESRRSSMASTSST-FFDTSSIGTVQNPYADVKTSLHDSQVptSNSNTSVQNMGNTDSVVYST 492
Cdd:pfam07489  80 NNTPAQGNTDTSGAEETASSRRSSQASTASTtWSDTSSIDTVQNPYADVGMSRNDSQA--RNPEEPIYDEVAADSPIYSV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833815   493 IQHPPRDTTDNGaRLLGNPSAGIQSTYARLALSGGLRHDMGGLTGGSNSAVNTSNNPPAPGSHRFV 558
Cdd:pfam07489 158 IQHFSGDTPDTG-RLLGNPGQGIQSTYALLASSGGLRLGMGGLTGGGESAVSTANAAPTPGSHRFV 222
Tir_receptor_M pfam03549
Translocated intimin receptor (Tir) intimin-binding domain; Intimin and its translocated ...
 269-333 1.19e-29

Translocated intimin receptor (Tir) intimin-binding domain; 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 localized 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.


Pssm-ID: 460968  Cd Length: 65  Bit Score: 111.02  E-value: 1.19e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833815   269 DAAASATETATRDQLTKEAFQNPDNQKVNIDELGNAIPSGVLKDDVVANIEEQAKAAGEEAKQQA 333
Cdd:pfam03549   1 DAAASAAETATKDQLTQEAFQNPDNQKVNIDENGNAIPSGELKDDVVAQIAEQAKAAGEEARQQA 65
 
Name Accession Description Interval E-value
Tir_receptor_N pfam07490
Translocated intimin receptor (Tir) N-terminus; Intimin and its translocated intimin receptor ...
 1-267 1.32e-150

Translocated intimin receptor (Tir) N-terminus; 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 localized 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.


Pssm-ID: 254231  Cd Length: 269  Bit Score: 432.84  E-value: 1.32e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815     1 MPIGNLGHNPNVNNSIPPAPPLPSQTDGA-GGRGQLINSTGPLGSRALFTPVRNSMADSGDNRASDVPGLPVNPMRLAAS 79
Cdd:pfam07490   1 MPIGNLGHNPNVNALIPPAPPLPSQTDGArGGRGQLISSTGALGSRLLFTPIRNSVADSVDSRASDIPGLPVNPLRLAAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815    80 EITLNDGFEVLHDHGPLDTLNRQIGSSVFRVETQEDGKHIAVGQRNGVETSVVLSDQEYARLQSIDPEGKDKFVFTGGRG 159
Cdd:pfam07490  81 EITLNGGFEVLHDKGPLDTLNTQIGSSAFRVETQDDGSHVAIGQKNGLETSVVLSEQEFSSLQAIDPEGKNRFVFTGGRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   160 GAGHAMVTVASDITEARQRILELLEPKGTGESKGAGeskgvgelRESNSGAENTTETQTST---------STSSLRSDPK 230
Cdd:pfam07490 161 GAGHAMVTVASDIAEARQRILDKLEPKDTGGRQAKD--------RTSNSGGVNSAEGQDDGtssethtstSTSSLRSDPK 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 15833815   231 LWLALGTVATGLIGLAATGIVQALALTPEPDSPTTTD 267
Cdd:pfam07490 233 LWLSLGTIAAGLIGLAATGIAQALALTPEPDDPTTTD 269
Tir_receptor_C pfam07489
Translocated intimin receptor (Tir) C-terminus; Intimin and its translocated intimin receptor ...
 334-558 2.09e-96

Translocated intimin receptor (Tir) C-terminus; 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 localized 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.


Pssm-ID: 369388  Cd Length: 222  Bit Score: 292.69  E-value: 2.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   334 IENNAQAQKKYDEQQAKRQEELKVSSGAGYGLSGALILGGGIGVAVTAALHRKNQPVEQTTTTTTTTTTTSArTVENKPA 413
Cdd:pfam07489   1 IESNAQAQQRYDEQQAKRQEELNLSSGAGYGLSGALILGGGIGAGVTAALHRRNQPVEQTTTTTTTTTTTST-TVENKPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833815   414 NNTPAQGNVDTPGSEDTMESRRSSMASTSST-FFDTSSIGTVQNPYADVKTSLHDSQVptSNSNTSVQNMGNTDSVVYST 492
Cdd:pfam07489  80 NNTPAQGNTDTSGAEETASSRRSSQASTASTtWSDTSSIDTVQNPYADVGMSRNDSQA--RNPEEPIYDEVAADSPIYSV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833815   493 IQHPPRDTTDNGaRLLGNPSAGIQSTYARLALSGGLRHDMGGLTGGSNSAVNTSNNPPAPGSHRFV 558
Cdd:pfam07489 158 IQHFSGDTPDTG-RLLGNPGQGIQSTYALLASSGGLRLGMGGLTGGGESAVSTANAAPTPGSHRFV 222
Tir_receptor_M pfam03549
Translocated intimin receptor (Tir) intimin-binding domain; Intimin and its translocated ...
 269-333 1.19e-29

Translocated intimin receptor (Tir) intimin-binding domain; 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 localized 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.


Pssm-ID: 460968  Cd Length: 65  Bit Score: 111.02  E-value: 1.19e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833815   269 DAAASATETATRDQLTKEAFQNPDNQKVNIDELGNAIPSGVLKDDVVANIEEQAKAAGEEAKQQA 333
Cdd:pfam03549   1 DAAASAAETATKDQLTQEAFQNPDNQKVNIDENGNAIPSGELKDDVVAQIAEQAKAAGEEARQQA 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH