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Conserved domains on  [gi|1248555041|ref|WP_096751918|]
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signal peptidase I [Burkholderia gladioli]

Protein Classification

S26 family signal peptidase( domain architecture ID 12106434)

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|GO:0016020|GO:0006508|GO:0008236
MEROPS:  S26
PubMed:  22031009|16126156|10982814

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 14-202 1.33e-47

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: 154.29  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  14 FIAFLFLMVIfRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYDIRipfthvrlvrlhEPQRGDIVTIDS-AAAHELLVK 92
Cdd:pfam10502   9 VIALLLALLI-RTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLG------------EPKRGDIVVFRPpEGPGVPLIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  93 RLIGLPGDTVAMHDNVLTINGKradyrPIGSNLLRSDADSPGEYLAERIGGAphtvrlspeapspresfgpiVVPPGQYL 172
Cdd:pfam10502  76 RVIGLPGDRVEYKDDQLYINGK-----PVGEPYLADRKGRPTFDLPPWQGCR--------------------VVPEGEYF 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 1248555041 173 MLGDNRDNSADSRYFGFFPRDEIMGRARRV 202
Cdd:pfam10502 131 VMGDNRDNSLDSRYFGFVPASNIVGRAVFP 160
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 14-202 1.33e-47

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: 154.29  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  14 FIAFLFLMVIfRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYDIRipfthvrlvrlhEPQRGDIVTIDS-AAAHELLVK 92
Cdd:pfam10502   9 VIALLLALLI-RTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLG------------EPKRGDIVVFRPpEGPGVPLIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  93 RLIGLPGDTVAMHDNVLTINGKradyrPIGSNLLRSDADSPGEYLAERIGGAphtvrlspeapspresfgpiVVPPGQYL 172
Cdd:pfam10502  76 RVIGLPGDRVEYKDDQLYINGK-----PVGEPYLADRKGRPTFDLPPWQGCR--------------------VVPEGEYF 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 1248555041 173 MLGDNRDNSADSRYFGFFPRDEIMGRARRV 202
Cdd:pfam10502 131 VMGDNRDNSLDSRYFGFVPASNIVGRAVFP 160
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 27-207 9.65e-43

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: 141.21  E-value: 9.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  27 AVADWNVVPSGSMLPTIRIGDRILVDKMAYdiripfthvrlvRLHEPQRGDIVTI-DSAAAHELLVKRLIGLPGDTVAMH 105
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAY------------RTSDPKRGDIVVFkDPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 106 DNVLTINGKRADYrpigsnllrsdadspgEYLAERigGAPHTVRLSpeapspresfGPIVVPPGQYLMLGDNRDNSADSR 185
Cdd:TIGR02227  69 DGKLYINGKKIDE----------------PYLKPN--GYLDTSEFN----------TPVKVPPGHYFVLGDNRDNSLDSR 120

                         170       180
                  ....*....|....*....|..
gi 1248555041 186 YFGFFPRDEIMGRARRVAFSLD 207
Cdd:TIGR02227 121 YFGFVPIDQIIGKVSFVFYPFD 142
PRK10861 PRK10861
signal peptidase I;
18-220 6.35e-39

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 136.72  E-value: 6.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  18 LFLMVIFRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYDIRIPFTHVRLVRLHEPQRGDIVTIDSAAAHEL-LVKRLIG 96
Cdd:PRK10861   71 LAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLdYIKRVVG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  97 LPGD--------------------------------TVAMHDNVLTINGKRADYRPIGSNLLRSDADSPGEY-LAERI-- 141
Cdd:PRK10861  151 LPGDkvtydpvskevtiqpgcssgqacenalpvtysNVEPSDFVQTFSRRNGGEATSGFFQVPLNETKENGIrLSERKet 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 142 -GGAPHTVRLSPEAPS--------PRESFGPIVVPPGQYLMLGDNRDNSADSRYFGFFPRDEIMGRARRVAFSLDPSRDY 212
Cdd:PRK10861  231 lGDVTHRILTVPGAQDqvgmyyqqPGQPLATWVVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQEGE 310

                         250
                  ....*....|.
gi 1248555041 213 LP---RLDRFG 220
Cdd:PRK10861  311 WPtgvRLSRIG 321
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
6-193 2.47e-32

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 116.11  E-value: 2.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041   6 RLWKANKGFIAFLFLMVIFRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYdiripfthvrlvRLHEPQRGDIVTIDS-A 84
Cdd:COG0681    10 ELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY------------GFGEPKRGDIVVFKYpE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  85 AAHELLVKRLIGLPGDTVAMHDNVLTINGKRADYRPIGSNLLRSDADSPGEYLAERIGGAPHTVRLSPEAPSPRESFGPI 164
Cdd:COG0681    78 DPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGG 157

                         170       180
                  ....*....|....*....|....*....
gi 1248555041 165 VVPPGQYLMLGDNRDNSADSRYFGFFPRD 193
Cdd:COG0681   158 GVGVDGVGVGGVVDVVVPDVDSRLVDVGD 186
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 31-199 5.25e-19

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: 78.40  E-value: 5.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  31 WNVVPSGSMLPTIRIGDRILVDKMAYDIRipfthvrlvrlhEPQRGDIVTIDS-AAAHELLVKRLIGlpgdtvamhdnvl 109
Cdd:cd06530     2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFR------------EPKRGDVVVFKSpGDPGKPIIKRVIG------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 110 tingkradyrpigsnllrsdadspgeylaeriggaphtvrlspeapspresfgpivvppgqYLMLGDNRDNSADSRYFGF 189
Cdd:cd06530    57 -------------------------------------------------------------YFVLGDNRNNSLDSRYWGP 75

                         170
                  ....*....|
gi 1248555041 190 FPRDEIMGRA 199
Cdd:cd06530    76 VPEDDIVGKV 85
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 14-202 1.33e-47

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: 154.29  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  14 FIAFLFLMVIfRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYDIRipfthvrlvrlhEPQRGDIVTIDS-AAAHELLVK 92
Cdd:pfam10502   9 VIALLLALLI-RTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLG------------EPKRGDIVVFRPpEGPGVPLIK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  93 RLIGLPGDTVAMHDNVLTINGKradyrPIGSNLLRSDADSPGEYLAERIGGAphtvrlspeapspresfgpiVVPPGQYL 172
Cdd:pfam10502  76 RVIGLPGDRVEYKDDQLYINGK-----PVGEPYLADRKGRPTFDLPPWQGCR--------------------VVPEGEYF 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 1248555041 173 MLGDNRDNSADSRYFGFFPRDEIMGRARRV 202
Cdd:pfam10502 131 VMGDNRDNSLDSRYFGFVPASNIVGRAVFP 160
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 27-207 9.65e-43

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: 141.21  E-value: 9.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  27 AVADWNVVPSGSMLPTIRIGDRILVDKMAYdiripfthvrlvRLHEPQRGDIVTI-DSAAAHELLVKRLIGLPGDTVAMH 105
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAY------------RTSDPKRGDIVVFkDPDTNKNIYVKRIIGLPGDKVEFR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 106 DNVLTINGKRADYrpigsnllrsdadspgEYLAERigGAPHTVRLSpeapspresfGPIVVPPGQYLMLGDNRDNSADSR 185
Cdd:TIGR02227  69 DGKLYINGKKIDE----------------PYLKPN--GYLDTSEFN----------TPVKVPPGHYFVLGDNRDNSLDSR 120

                         170       180
                  ....*....|....*....|..
gi 1248555041 186 YFGFFPRDEIMGRARRVAFSLD 207
Cdd:TIGR02227 121 YFGFVPIDQIIGKVSFVFYPFD 142
PRK10861 PRK10861
signal peptidase I;
18-220 6.35e-39

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 136.72  E-value: 6.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  18 LFLMVIFRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYDIRIPFTHVRLVRLHEPQRGDIVTIDSAAAHEL-LVKRLIG 96
Cdd:PRK10861   71 LAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPITQTTLIETGHPKRGDIVVFKYPEDPKLdYIKRVVG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  97 LPGD--------------------------------TVAMHDNVLTINGKRADYRPIGSNLLRSDADSPGEY-LAERI-- 141
Cdd:PRK10861  151 LPGDkvtydpvskevtiqpgcssgqacenalpvtysNVEPSDFVQTFSRRNGGEATSGFFQVPLNETKENGIrLSERKet 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 142 -GGAPHTVRLSPEAPS--------PRESFGPIVVPPGQYLMLGDNRDNSADSRYFGFFPRDEIMGRARRVAFSLDPSRDY 212
Cdd:PRK10861  231 lGDVTHRILTVPGAQDqvgmyyqqPGQPLATWVVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQEGE 310

                         250
                  ....*....|.
gi 1248555041 213 LP---RLDRFG 220
Cdd:PRK10861  311 WPtgvRLSRIG 321
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
6-193 2.47e-32

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 116.11  E-value: 2.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041   6 RLWKANKGFIAFLFLMVIFRSAVADWNVVPSGSMLPTIRIGDRILVDKMAYdiripfthvrlvRLHEPQRGDIVTIDS-A 84
Cdd:COG0681    10 ELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSY------------GFGEPKRGDIVVFKYpE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  85 AAHELLVKRLIGLPGDTVAMHDNVLTINGKRADYRPIGSNLLRSDADSPGEYLAERIGGAPHTVRLSPEAPSPRESFGPI 164
Cdd:COG0681    78 DPSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNEPYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGG 157

                         170       180
                  ....*....|....*....|....*....
gi 1248555041 165 VVPPGQYLMLGDNRDNSADSRYFGFFPRD 193
Cdd:COG0681   158 GVGVDGVGVGGVVDVVVPDVDSRLVDVGD 186
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 75-202 1.54e-24

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: 93.44  E-value: 1.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  75 RGDIVTIDSAA----------AHELLVKRLIGLPGDTVAMHDNVLTINGKradyrPIGSNLLRsdaDSPGEylaerigga 144
Cdd:COG4959     1 RGDLVAFRPPEplaaergylpRGVPLIKRVAALPGDTVCIKGGQVYINGK-----PVAEALER---DRAGR--------- 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1248555041 145 phtvrlspeaPSPRESfGPIVVPPGQYLMLGDNRDNSADSRYFGFFPRDEIMGRARRV 202
Cdd:COG4959    64 ----------PLPVWQ-GCGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPL 110
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 31-199 5.25e-19

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: 78.40  E-value: 5.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  31 WNVVPSGSMLPTIRIGDRILVDKMAYDIRipfthvrlvrlhEPQRGDIVTIDS-AAAHELLVKRLIGlpgdtvamhdnvl 109
Cdd:cd06530     2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFR------------EPKRGDVVVFKSpGDPGKPIIKRVIG------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 110 tingkradyrpigsnllrsdadspgeylaeriggaphtvrlspeapspresfgpivvppgqYLMLGDNRDNSADSRYFGF 189
Cdd:cd06530    57 -------------------------------------------------------------YFVLGDNRNNSLDSRYWGP 75

                         170
                  ....*....|
gi 1248555041 190 FPRDEIMGRA 199
Cdd:cd06530    76 VPEDDIVGKV 85
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 33-199 7.43e-11

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: 56.50  E-value: 7.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  33 VVPSGSMLPTIRIGDRILVDKMAYDiripfthvrlvrlhePQRGDIVTIDSaAAHELLVKRLIGLPGdtvamhdnvltin 112
Cdd:cd06462     4 RVEGDSMEPTIPDGDLVLVDKSSYE---------------PKRGDIVVFRL-PGGELTVKRVIGLPG------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041 113 gkradyrpigsnllrsdadspgeylaeriggaphtvrlspeapspresfgpivvpPGQYLMLGDNrDNSADSRYFGfFPR 192
Cdd:cd06462    55 -------------------------------------------------------EGHYFLLGDN-PNSPDSRIDG-PPE 77


                  ....*..
gi 1248555041 193 DEIMGRA 199
Cdd:cd06462    78 LDIVGVV 84
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 75-202 2.87e-08

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: 51.71  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  75 RGDIVTIDSAAAHELLVKRLIGLPGDTVAMHDNVLTINGKRADYrpigsnllrsdadspgeylaerigGAPHTVRLSPEA 154
Cdd:TIGR02771  69 RGYLREGLCPGGFGPLLKRVLGLPGDRVTVRADVVAINGQLLPY------------------------SKPLATDSSGRP 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1248555041 155 PSPresFGPIVVPPGqYLMLGDNRDNSADSRYFGFFPRDEIMGRARRV 202
Cdd:TIGR02771 125 LPP---FPEGVIPPG-FFVVHDTSPTSFDSRYFGPISREQVIGRVKPL 168
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 90-208 5.65e-06

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 45.37  E-value: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  90 LVKRLIGLPGDTVAMHDNVlTINGkradyRPIGSNLLRSdADSPGEYLAERIGGaphtvrlspeapspresfgpiVVPPG 169
Cdd:PRK13838   88 LIKTVAALAGQRVEIGGSV-SIDG-----RPLPSSSVRR-RDGEGRPLTPFPGG---------------------VVPPG 139

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1248555041 170 qYLMLGDNRDNSADSRYFGFFPRDEIMGRARRVaFSLDP 208
Cdd:PRK13838  140 -HLFLHSSFAGSYDSRYFGPVPASGLLGLARPV-LTFDP 176
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 38-121 1.09e-03

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 37.63  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248555041  38 SMLPTIRIGDRILVDKMAYDIRipfthvrlvrlhepqRGDIVTIDSaaAHELLVKRLIGLPGDTVAMH-DNvltingkrA 116
Cdd:COG2932    44 SMEPTIRDGDIVLVDPSDTEIR---------------DGGIYVVRT--DGELLVKRLQRRPDGKLRLIsDN--------P 98


                  ....*
gi 1248555041 117 DYRPI 121
Cdd:COG2932    99 AYPPI 103
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 157-200 4.07e-03

nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair]


Pssm-ID: 274282 [Multi-domain]  Cd Length: 90  Bit Score: 35.51  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1248555041 157 PRESFGPIV-----VPPGQYLMLGDNRDNSADSRYFGFFPRDEIMGRAR 200
Cdd:TIGR02754  41 PLQPYGLIIkrlaaVDDNGLFLLGDNPKASTDSRQLGPVPRSLLLGKVL 89
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 38-102 4.74e-03

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: 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 LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are 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. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 34.84  E-value: 4.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248555041  38 SMLPTIRIGDRILVDkmaydiripfthvrlvRLHEPQRGDIVtidsAAAH--ELLVKRLIGLPGDTV 102
Cdd:cd06529     9 SMEPTIPDGDLVLVD----------------PSDTPRDGDIV----VARLdgELTVKRLQRRGGGRL 55
 
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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