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Conserved domains on  [gi|2335313853|ref|WP_265856647|]
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signal peptidase I [Bombilactobacillus mellis]

Protein Classification

S26 family signal peptidase( domain architecture ID 1011306)

S26 family signal peptidase is a membrane-bound serine protease which frees proteins tethered to inner or mitochondrial membranes by cleaving off signal peptides during polypeptide translocation

EC:  3.4.21.-
Gene Ontology:  GO:0004252|GO:0006465
MEROPS:  S26
PubMed:  10982814

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S26 super family cl37809
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 11-207 7.63e-19

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


The actual alignment was detected with superfamily member pfam10502:

Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 80.33  E-value: 7.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  11 WFLTILWFLILIGFV--MIFSPIKIHGNSMENSYKNNqilwglNYRLknpfnHNFFGPKLFSIQRNDVLVIDSKKFENMe 88
Cdd:pfam10502   4 WVKAIVIALLLALLIrtFLFEPYVVPGGSMSPTLPIG------DYLI-----VNKFSYGLGEPKRGDIVVFRPPEGPGV- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  89 krqnnapnPLIKRVIALPKETIEIKKHVVFLNGKVLHETYISKShffdnvTGQITnkSKFPYLIRERmfrnntlnnqnis 168
Cdd:pfam10502  72 --------PLIKRVIGLPGDRVEYKDDQLYINGKPVGEPYLADR------KGRPT--FDLPPWQGCR------------- 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2335313853 169 vRLGNDQFFAMGDNRNYSWDSRVYGSFNINNEV-KAKIIH 207
Cdd:pfam10502 123 -VVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVgRAVFPV 161
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 11-207 7.63e-19

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 80.33  E-value: 7.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  11 WFLTILWFLILIGFV--MIFSPIKIHGNSMENSYKNNqilwglNYRLknpfnHNFFGPKLFSIQRNDVLVIDSKKFENMe 88
Cdd:pfam10502   4 WVKAIVIALLLALLIrtFLFEPYVVPGGSMSPTLPIG------DYLI-----VNKFSYGLGEPKRGDIVVFRPPEGPGV- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  89 krqnnapnPLIKRVIALPKETIEIKKHVVFLNGKVLHETYISKShffdnvTGQITnkSKFPYLIRERmfrnntlnnqnis 168
Cdd:pfam10502  72 --------PLIKRVIGLPGDRVEYKDDQLYINGKPVGEPYLADR------KGRPT--FDLPPWQGCR------------- 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2335313853 169 vRLGNDQFFAMGDNRNYSWDSRVYGSFNINNEV-KAKIIH 207
Cdd:pfam10502 123 -VVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVgRAVFPV 161
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 73-193 1.66e-16

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 72.64  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  73 RNDVLVIDSKKFENMEKRQNNAPNPLIKRVIALPKETIEIKKHVVFLNGKVLHETyiskshffdnvtgqitnkskfpyLI 152
Cdd:COG4959     1 RGDLVAFRPPEPLAAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEA-----------------------LE 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2335313853 153 RERMFRNntLNNQNISVRLGNDQFFAMGDNRNYSWDSRVYG 193
Cdd:COG4959    58 RDRAGRP--LPVWQGCGVVPEGEYFLLGDNRPNSFDSRYFG 96
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 27-206 3.15e-16

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 72.65  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  27 IFSPIKIHGNSMENSYKNNQilWGLNYRLKNPFNhnffgpklfSIQRNDVLVIDSKkfenmekrqNNAPNPLIKRVIALP 106
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGD--RILVNKFAYRTS---------DPKRGDIVVFKDP---------DTNKNIYVKRIIGLP 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853 107 KETIEIKKHVVFLNGKVLHETYISKshffdnvtGQITNKSKFPYLirermfrnntlnnqnisVRLGNDQFFAMGDNRNYS 186
Cdd:TIGR02227  62 GDKVEFRDGKLYINGKKIDEPYLKP--------NGYLDTSEFNTP-----------------VKVPPGHYFVLGDNRDNS 116

                         170       180
                  ....*....|....*....|
gi 2335313853 187 WDSRVYGSFNINNeVKAKII 206
Cdd:TIGR02227 117 LDSRYFGFVPIDQ-IIGKVS 135
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 29-205 7.30e-04

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 37.57  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  29 SPIKIHGNSMENSYKNNQILwglnyrLKNPFNHNFFGPKlfsiqRNDVLVIDSKKfenmekrqnNAPNPLIKRVIAlpke 108
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLV------LVNKLSYGFREPK-----RGDVVVFKSPG---------DPGKPIIKRVIG---- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853 109 tieikkhvvflngkvlhetyiskshffdnvtgqitnkskfpylirermfrnntlnnqnisvrlgndqFFAMGDNRNYSWD 188
Cdd:cd06530    57 -------------------------------------------------------------------YFVLGDNRNNSLD 69

                         170
                  ....*....|....*..
gi 2335313853 189 SRVYGSFNINNeVKAKI 205
Cdd:cd06530    70 SRYWGPVPEDD-IVGKV 85
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 11-207 7.63e-19

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 80.33  E-value: 7.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  11 WFLTILWFLILIGFV--MIFSPIKIHGNSMENSYKNNqilwglNYRLknpfnHNFFGPKLFSIQRNDVLVIDSKKFENMe 88
Cdd:pfam10502   4 WVKAIVIALLLALLIrtFLFEPYVVPGGSMSPTLPIG------DYLI-----VNKFSYGLGEPKRGDIVVFRPPEGPGV- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  89 krqnnapnPLIKRVIALPKETIEIKKHVVFLNGKVLHETYISKShffdnvTGQITnkSKFPYLIRERmfrnntlnnqnis 168
Cdd:pfam10502  72 --------PLIKRVIGLPGDRVEYKDDQLYINGKPVGEPYLADR------KGRPT--FDLPPWQGCR------------- 122

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2335313853 169 vRLGNDQFFAMGDNRNYSWDSRVYGSFNINNEV-KAKIIH 207
Cdd:pfam10502 123 -VVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVgRAVFPV 161
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 73-193 1.66e-16

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 72.64  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  73 RNDVLVIDSKKFENMEKRQNNAPNPLIKRVIALPKETIEIKKHVVFLNGKVLHETyiskshffdnvtgqitnkskfpyLI 152
Cdd:COG4959     1 RGDLVAFRPPEPLAAERGYLPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEA-----------------------LE 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2335313853 153 RERMFRNntLNNQNISVRLGNDQFFAMGDNRNYSWDSRVYG 193
Cdd:COG4959    58 RDRAGRP--LPVWQGCGVVPEGEYFLLGDNRPNSFDSRYFG 96
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
11-198 2.43e-16

Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 74.12  E-value: 2.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  11 WFLTILWFLILIGFV--MIFSPIKIHGNSMENSYKNNQILWG--LNYRLKNPfnhnffgpklfsiQRNDVLVIDSKKfen 86
Cdd:COG0681    14 WLKSIVIALLLALLIrtFVFEPFVIPSGSMEPTLLVGDRLLVnkLSYGFGEP-------------KRGDIVVFKYPE--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  87 mekrqnNAPNPLIKRVIALPKETIEIKKHVVFLNGKVLHETYISKSHFFDNVTGQITNKSKFPYLI-----RERMFRNNT 161
Cdd:COG0681    78 ------DPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEEVPggggdNSNDSRSGD 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2335313853 162 LNNQNISVRLGNDQFFAMGDNRNYSWDSRVYGSFNIN 198
Cdd:COG0681   152 PDDGGGGVGVDGVGVGGVVDVVVPDVDSRLVDVGDGP 188
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 27-206 3.15e-16

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 72.65  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  27 IFSPIKIHGNSMENSYKNNQilWGLNYRLKNPFNhnffgpklfSIQRNDVLVIDSKkfenmekrqNNAPNPLIKRVIALP 106
Cdd:TIGR02227   2 VFFPYKIPGGSMEPTLKEGD--RILVNKFAYRTS---------DPKRGDIVVFKDP---------DTNKNIYVKRIIGLP 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853 107 KETIEIKKHVVFLNGKVLHETYISKshffdnvtGQITNKSKFPYLirermfrnntlnnqnisVRLGNDQFFAMGDNRNYS 186
Cdd:TIGR02227  62 GDKVEFRDGKLYINGKKIDEPYLKP--------NGYLDTSEFNTP-----------------VKVPPGHYFVLGDNRDNS 116

                         170       180
                  ....*....|....*....|
gi 2335313853 187 WDSRVYGSFNINNeVKAKII 206
Cdd:TIGR02227 117 LDSRYFGFVPIDQ-IIGKVS 135
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 29-205 7.30e-04

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 37.57  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853  29 SPIKIHGNSMENSYKNNQILwglnyrLKNPFNHNFFGPKlfsiqRNDVLVIDSKKfenmekrqnNAPNPLIKRVIAlpke 108
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLV------LVNKLSYGFREPK-----RGDVVVFKSPG---------DPGKPIIKRVIG---- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335313853 109 tieikkhvvflngkvlhetyiskshffdnvtgqitnkskfpylirermfrnntlnnqnisvrlgndqFFAMGDNRNYSWD 188
Cdd:cd06530    57 -------------------------------------------------------------------YFVLGDNRNNSLD 69

                         170
                  ....*....|....*..
gi 2335313853 189 SRVYGSFNINNeVKAKI 205
Cdd:cd06530    70 SRYWGPVPEDD-IVGKV 85
 
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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