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Conserved domains on  [gi|446595110|ref|WP_000672456|]
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MULTISPECIES: S26 family signal peptidase [Gammaproteobacteria]

Protein Classification

S26 family signal peptidase( domain architecture ID 10008982)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 69-176 1.17e-27

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: 99.98  E-value: 1.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110  69 RGAVYAFHAKNM----QPFYKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVGEGLqLAGKLHLPESHFYGKATLKENN 144
Cdd:COG4959    1 RGDLVAFRPPEPlaaeRGYLPRGVPLIKRVAALPGDTVCIKGG-QVYINGKPVAEAL-ERDRAGRPLPVWQGCGVVPEGE 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446595110 145 YWFMG-KSLFSFDSRYWGTVKNDQIIGRAYPLF 176
Cdd:COG4959   79 YFLLGdNRPNSFDSRYFGPVPRSQIIGRAVPLW 111
 
Name Accession Description Interval E-value
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 69-176 1.17e-27

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: 99.98  E-value: 1.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110  69 RGAVYAFHAKNM----QPFYKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVGEGLqLAGKLHLPESHFYGKATLKENN 144
Cdd:COG4959    1 RGDLVAFRPPEPlaaeRGYLPRGVPLIKRVAALPGDTVCIKGG-QVYINGKPVAEAL-ERDRAGRPLPVWQGCGVVPEGE 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446595110 145 YWFMG-KSLFSFDSRYWGTVKNDQIIGRAYPLF 176
Cdd:COG4959   79 YFLLGdNRPNSFDSRYFGPVPRSQIIGRAVPLW 111
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 66-172 1.91e-18

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: 77.63  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110   66 SLERGAVYAFHAKNmqpfyKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVGEGLQLAGKLHLPES--HFYGKATLKEN 143
Cdd:pfam10502  54 EPKRGDIVVFRPPE-----GPGVPLIKRVIGLPGDRVEYKDD-QLYINGKPVGEPYLADRKGRPTFDlpPWQGCRVVPEG 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 446595110  144 NYWFMG-KSLFSFDSRYWGTVKNDQIIGRA 172
Cdd:pfam10502 128 EYFVMGdNRDNSLDSRYFGFVPASNIVGRA 157
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 60-172 1.91e-13

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: 63.79  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110   60 IDLKDQSLERGAVYAFHAKNmqpfyKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVgEGLQLAGKLHLPESHFYGKAT 139
Cdd:TIGR02227  28 FAYRTSDPKRGDIVVFKDPD-----TNKNIYVKRIIGLPGDKVEFRDG-KLYINGKKI-DEPYLKPNGYLDTSEFNTPVK 100

                          90       100       110
                  ....*....|....*....|....*....|....
gi 446595110  140 LKENNYWFMGKSL-FSFDSRYWGTVKNDQIIGRA 172
Cdd:TIGR02227 101 VPPGHYFVLGDNRdNSLDSRYFGFVPIDQIIGKV 134
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 145-172 9.90e-05

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: 39.11  E-value: 9.90e-05
                         10        20
                 ....*....|....*....|....*....
gi 446595110 145 YWFMG-KSLFSFDSRYWGTVKNDQIIGRA 172
Cdd:cd06530   57 YFVLGdNRNNSLDSRYWGPVPEDDIVGKV 85
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
 90-176 2.26e-03

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 36.93  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110  90 MVKILTGMPGDKVEINDKwKITVNGDVVG-EGLQLAGKLHLPESHFYG-KATLKENNYWFMG-KSLFSFDSRYWGTVKND 166
Cdd:PRK13884  88 MMKRVLAAKGDAVSVTDD-GVRVNGELLPlSKPILADGAGRPLPRYQAnSYTLGESELLLMSdVSATSFDGRYFGPINRS 166

                         90
                 ....*....|
gi 446595110 167 QIIGRAYPLF 176
Cdd:PRK13884 167 QIKTVIRPVI 176
 
Name Accession Description Interval E-value
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 69-176 1.17e-27

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: 99.98  E-value: 1.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110  69 RGAVYAFHAKNM----QPFYKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVGEGLqLAGKLHLPESHFYGKATLKENN 144
Cdd:COG4959    1 RGDLVAFRPPEPlaaeRGYLPRGVPLIKRVAALPGDTVCIKGG-QVYINGKPVAEAL-ERDRAGRPLPVWQGCGVVPEGE 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446595110 145 YWFMG-KSLFSFDSRYWGTVKNDQIIGRAYPLF 176
Cdd:COG4959   79 YFLLGdNRPNSFDSRYFGPVPRSQIIGRAVPLW 111
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 66-172 1.91e-18

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: 77.63  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110   66 SLERGAVYAFHAKNmqpfyKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVGEGLQLAGKLHLPES--HFYGKATLKEN 143
Cdd:pfam10502  54 EPKRGDIVVFRPPE-----GPGVPLIKRVIGLPGDRVEYKDD-QLYINGKPVGEPYLADRKGRPTFDlpPWQGCRVVPEG 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 446595110  144 NYWFMG-KSLFSFDSRYWGTVKNDQIIGRA 172
Cdd:pfam10502 128 EYFVMGdNRDNSLDSRYFGFVPASNIVGRA 157
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 60-172 1.91e-13

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: 63.79  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110   60 IDLKDQSLERGAVYAFHAKNmqpfyKDGTRMVKILTGMPGDKVEINDKwKITVNGDVVgEGLQLAGKLHLPESHFYGKAT 139
Cdd:TIGR02227  28 FAYRTSDPKRGDIVVFKDPD-----TNKNIYVKRIIGLPGDKVEFRDG-KLYINGKKI-DEPYLKPNGYLDTSEFNTPVK 100

                          90       100       110
                  ....*....|....*....|....*....|....
gi 446595110  140 LKENNYWFMGKSL-FSFDSRYWGTVKNDQIIGRA 172
Cdd:TIGR02227 101 VPPGHYFVLGDNRdNSLDSRYFGFVPIDQIIGKV 134
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 23-176 5.19e-09

conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding elements of conjugative transfer systems. This family is homologous to a broader family of signal (leader) peptidases such as lepB. This family is present in both Ti-type and I-type conjugative systems.


Pssm-ID: 131818 [Multi-domain]  Cd Length: 171  Bit Score: 52.87  E-value: 5.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110   23 GVTLLVLwgAGAAFASRYRIGIDPQQEKCLPGYTFFLIDLKDqsLERGAVYAFHAKNMQPFYKDGTR------------- 89
Cdd:TIGR02771   7 GIAGLAL--SGLTILGLYCVGARINTTKSLPLGLYWTTSSKP--VERGDYVVFCPPDNPQFEEARERgylreglcpggfg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110   90 -MVKILTGMPGDKVEINDKwKITVNGDVVGEGLQLA---GKLHLPESHfygkATLKENNYWFM-GKSLFSFDSRYWGTVK 164
Cdd:TIGR02771  83 pLLKRVLGLPGDRVTVRAD-VVAINGQLLPYSKPLAtdsSGRPLPPFP----EGVIPPGFFVVhDTSPTSFDSRYFGPIS 157

                         170
                  ....*....|..
gi 446595110  165 NDQIIGRAYPLF 176
Cdd:TIGR02771 158 REQVIGRVKPLF 169
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 145-172 9.90e-05

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: 39.11  E-value: 9.90e-05
                         10        20
                 ....*....|....*....|....*....
gi 446595110 145 YWFMG-KSLFSFDSRYWGTVKNDQIIGRA 172
Cdd:cd06530   57 YFVLGdNRNNSLDSRYWGPVPEDDIVGKV 85
PRK13884 PRK13884
conjugal transfer peptidase TraF; Provisional
 90-176 2.26e-03

conjugal transfer peptidase TraF; Provisional


Pssm-ID: 184368  Cd Length: 178  Bit Score: 36.93  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446595110  90 MVKILTGMPGDKVEINDKwKITVNGDVVG-EGLQLAGKLHLPESHFYG-KATLKENNYWFMG-KSLFSFDSRYWGTVKND 166
Cdd:PRK13884  88 MMKRVLAAKGDAVSVTDD-GVRVNGELLPlSKPILADGAGRPLPRYQAnSYTLGESELLLMSdVSATSFDGRYFGPINRS 166

                         90
                 ....*....|
gi 446595110 167 QIIGRAYPLF 176
Cdd:PRK13884 167 QIKTVIRPVI 176
 
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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