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Conserved domains on  [gi|1020087807|ref|WP_063224542|]
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MULTISPECIES: signal peptidase I [Bacillus]

Protein Classification

S26 family signal peptidase( domain architecture ID 10797859)

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
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 6-169 2.95e-60

signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, a subunit of the eukaryotic endoplasmic reticulum signal peptidase I complex, and an apparent signal peptidase I from a small number of bacteria. It is related to but does not overlap in hits with TIGR02227, the bacterial and mitochondrial signal peptidase I.


:

Pssm-ID: 131283  Cd Length: 158  Bit Score: 184.95  E-value: 2.95e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807   6 KVISNVISFVLFALMVCLAFVVISSKASGGDPTVMgyqfksVLSGSMEPTFLTGSIIAIEPKkDGSKYQKGDVITFKEKD 85
Cdd:TIGR02228   1 KKISNVIYFILIILLVILLLYGLVSKASGPDPVVV------VLSGSMEPTFNTGDLILVTGA-DPNDIQVGDVITYKSPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  86 E-KIITHRIIGVKDTNGKVMYETKGDNNNGPDLEPVLAENVIGKYADITVPYAGYALNYANSKAGAALLLIIPGVFLLGY 164
Cdd:TIGR02228  74 FnTPVTHRVIEINNSGGELGFITKGDNNPAPDGEPVPSENVIGKYLGFTIPFAGYVLVFAPQAIGAAALLIIPGIGLISY 153


                  ....*
gi 1020087807 165 SAISI 169
Cdd:TIGR02228 154 LFITI 158
 
Name Accession Description Interval E-value
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 6-169 2.95e-60

signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, a subunit of the eukaryotic endoplasmic reticulum signal peptidase I complex, and an apparent signal peptidase I from a small number of bacteria. It is related to but does not overlap in hits with TIGR02227, the bacterial and mitochondrial signal peptidase I.


Pssm-ID: 131283  Cd Length: 158  Bit Score: 184.95  E-value: 2.95e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807   6 KVISNVISFVLFALMVCLAFVVISSKASGGDPTVMgyqfksVLSGSMEPTFLTGSIIAIEPKkDGSKYQKGDVITFKEKD 85
Cdd:TIGR02228   1 KKISNVIYFILIILLVILLLYGLVSKASGPDPVVV------VLSGSMEPTFNTGDLILVTGA-DPNDIQVGDVITYKSPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  86 E-KIITHRIIGVKDTNGKVMYETKGDNNNGPDLEPVLAENVIGKYADITVPYAGYALNYANSKAGAALLLIIPGVFLLGY 164
Cdd:TIGR02228  74 FnTPVTHRVIEINNSGGELGFITKGDNNPAPDGEPVPSENVIGKYLGFTIPFAGYVLVFAPQAIGAAALLIIPGIGLISY 153


                  ....*
gi 1020087807 165 SAISI 169
Cdd:TIGR02228 154 LFITI 158
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 43-128 5.15e-16

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: 69.54  E-value: 5.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  43 QFKSVLSGSMEPTFLTGSIIAIEP-KKDGSKYQKGDVITFK--EKDEKIITHRIIGvkdtngkvmYETKGDNNNG----P 115
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKlSYGFREPKRGDVVVFKspGDPGKPIIKRVIG---------YFVLGDNRNNsldsR 71

                          90
                  ....*....|...
gi 1020087807 116 DLEPVLAENVIGK 128
Cdd:cd06530    72 YWGPVPEDDIVGK 84
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
1-96 1.23e-04

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 40.99  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807   1 MKLIWKVISNVISFVL-FALMVCLAFVVISskasggdptvMGYQFKSVLSGSMEPTFLTGSIIAIEP-KKDGSKYQKGDV 78
Cdd:COG0681     1 MSKKKKKKRELREWLKsIVIALLLALLIRT----------FVFEPFVIPSGSMEPTLLVGDRLLVNKlSYGFGEPKRGDI 70

                          90       100
                  ....*....|....*....|
gi 1020087807  79 ITFK--EKDEKIITHRIIGV 96
Cdd:COG0681    71 VVFKypEDPSKDYIKRVIGL 90
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 12-129 4.97e-04

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: 38.73  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  12 ISFVLFALMVCLAFVVISskasggdptVMGYQFKSVLSGSMEPTFLTGSIIaIEPK--KDGSKYQKGDVITFK--EKDEK 87
Cdd:pfam10502   2 LEWVKAIVIALLLALLIR---------TFLFEPYVVPGGSMSPTLPIGDYL-IVNKfsYGLGEPKRGDIVVFRppEGPGV 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1020087807  88 IITHRIIGVK-DT----------NGKVM---YETKGDNNNGPDLEPVLAENVI--GKY 129
Cdd:pfam10502  72 PLIKRVIGLPgDRveykddqlyiNGKPVgepYLADRKGRPTFDLPPWQGCRVVpeGEY 129
 
Name Accession Description Interval E-value
sigpep_I_arch TIGR02228
signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, ...
 6-169 2.95e-60

signal peptidase I, archaeal type; This model represents signal peptidase I from most archaea, a subunit of the eukaryotic endoplasmic reticulum signal peptidase I complex, and an apparent signal peptidase I from a small number of bacteria. It is related to but does not overlap in hits with TIGR02227, the bacterial and mitochondrial signal peptidase I.


Pssm-ID: 131283  Cd Length: 158  Bit Score: 184.95  E-value: 2.95e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807   6 KVISNVISFVLFALMVCLAFVVISSKASGGDPTVMgyqfksVLSGSMEPTFLTGSIIAIEPKkDGSKYQKGDVITFKEKD 85
Cdd:TIGR02228   1 KKISNVIYFILIILLVILLLYGLVSKASGPDPVVV------VLSGSMEPTFNTGDLILVTGA-DPNDIQVGDVITYKSPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  86 E-KIITHRIIGVKDTNGKVMYETKGDNNNGPDLEPVLAENVIGKYADITVPYAGYALNYANSKAGAALLLIIPGVFLLGY 164
Cdd:TIGR02228  74 FnTPVTHRVIEINNSGGELGFITKGDNNPAPDGEPVPSENVIGKYLGFTIPFAGYVLVFAPQAIGAAALLIIPGIGLISY 153


                  ....*
gi 1020087807 165 SAISI 169
Cdd:TIGR02228 154 LFITI 158
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 43-128 5.15e-16

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: 69.54  E-value: 5.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  43 QFKSVLSGSMEPTFLTGSIIAIEP-KKDGSKYQKGDVITFK--EKDEKIITHRIIGvkdtngkvmYETKGDNNNG----P 115
Cdd:cd06530     1 EPVVVPGGSMEPTLQPGDLVLVNKlSYGFREPKRGDVVVFKspGDPGKPIIKRVIG---------YFVLGDNRNNsldsR 71

                          90
                  ....*....|...
gi 1020087807 116 DLEPVLAENVIGK 128
Cdd:cd06530    72 YWGPVPEDDIVGK 84
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 47-128 2.42e-13

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 62.28  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  47 VLSGSMEPTFLTGSIIAIEpkKDGSKYQKGDVITFKEKDEKIITHRIIGVKDTNGkvmYETKGDNNNGPD--LEPVLAEN 124
Cdd:cd06462     5 VEGDSMEPTIPDGDLVLVD--KSSYEPKRGDIVVFRLPGGELTVKRVIGLPGEGH---YFLLGDNPNSPDsrIDGPPELD 79


                  ....
gi 1020087807 125 VIGK 128
Cdd:cd06462    80 IVGV 83
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
1-96 1.23e-04

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 40.99  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807   1 MKLIWKVISNVISFVL-FALMVCLAFVVISskasggdptvMGYQFKSVLSGSMEPTFLTGSIIAIEP-KKDGSKYQKGDV 78
Cdd:COG0681     1 MSKKKKKKRELREWLKsIVIALLLALLIRT----------FVFEPFVIPSGSMEPTLLVGDRLLVNKlSYGFGEPKRGDI 70

                          90       100
                  ....*....|....*....|
gi 1020087807  79 ITFK--EKDEKIITHRIIGV 96
Cdd:COG0681    71 VVFKypEDPSKDYIKRVIGL 90
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 42-129 4.81e-04

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: 38.75  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  42 YQFKSVLSGSMEPTFLTGS-IIAIEPKKDGSKYQKGDVITFKEKDE--KIITHRIIGVK-DT----------NGKVMYET 107
Cdd:TIGR02227   3 FFPYKIPGGSMEPTLKEGDrILVNKFAYRTSDPKRGDIVVFKDPDTnkNIYVKRIIGLPgDKvefrdgklyiNGKKIDEP 82

                          90       100
                  ....*....|....*....|....
gi 1020087807 108 KGDNNNGPDLEPVLAENVI--GKY 129
Cdd:TIGR02227  83 YLKPNGYLDTSEFNTPVKVppGHY 106
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 12-129 4.97e-04

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: 38.73  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020087807  12 ISFVLFALMVCLAFVVISskasggdptVMGYQFKSVLSGSMEPTFLTGSIIaIEPK--KDGSKYQKGDVITFK--EKDEK 87
Cdd:pfam10502   2 LEWVKAIVIALLLALLIR---------TFLFEPYVVPGGSMSPTLPIGDYL-IVNKfsYGLGEPKRGDIVVFRppEGPGV 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1020087807  88 IITHRIIGVK-DT----------NGKVM---YETKGDNNNGPDLEPVLAENVI--GKY 129
Cdd:pfam10502  72 PLIKRVIGLPgDRveykddqlyiNGKPVgepYLADRKGRPTFDLPPWQGCRVVpeGEY 129
 
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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