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Conserved domains on  [gi|365233140|gb|EHM74102|]
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signal peptidase I [Staphylococcus epidermidis 14.1.R1.SE]

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 ...
 21-176 6.41e-55

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: 171.62  E-value: 6.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   21 LVQKFLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGKPGDSVEYKKDQLYLNG 98
Cdd:pfam10502  17 LIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPpeGPGVPLIKRVIGLPGDRVEYKDDQLYING 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365233140   99 KKVDEPYLSENKKHkvgeyltenfNSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKVVLRYW 176
Cdd:pfam10502  97 KPVGEPYLADRKGR----------PTFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRY--FGFVPASNIVGRAVFPVW 162
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 21-176 6.41e-55

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: 171.62  E-value: 6.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   21 LVQKFLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGKPGDSVEYKKDQLYLNG 98
Cdd:pfam10502  17 LIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPpeGPGVPLIKRVIGLPGDRVEYKDDQLYING 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365233140   99 KKVDEPYLSENKKHkvgeyltenfNSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKVVLRYW 176
Cdd:pfam10502  97 KPVGEPYLADRKGR----------PTFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRY--FGFVPASNIVGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 25-179 1.45e-48

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: 154.69  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   25 FLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGKPGDSVEYKKDQLYLNGKKVD 102
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDpdTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 365233140  103 EPYLSENKkhkvgeyltenfnSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKVVLRYWPFN 179
Cdd:TIGR02227  81 EPYLKPNG-------------YLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRY--FGFVPIDQIIGKVSFVFYPFD 142
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
2-187 2.57e-30

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 109.56  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   2 KKEIIEWIVAIIVAIVIVTLVQKFLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRL 79
Cdd:COG0681    8 KRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYpeDPSKDYIKRV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  80 IGKPGDSVEYKKDQLYLNGKKVDEPYLsenkkhkvGEYLTENFNSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMDEV 159
Cdd:COG0681   88 IGLPGDTVEIRDGQVYVNGKPLNEPYL--------EEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGV 159

                        170       180
                 ....*....|....*....|....*...
gi 365233140 160 GLLDKNQVVGKVVLRYWPFNRWGGSFNP 187
Cdd:COG0681  160 GVDGVGVGGVVDVVVPDVDSRLVDVGDG 187
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 30-171 2.03e-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: 70.69  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  30 YTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGkpgdsveykkdqlylngkkvdepyls 107
Cdd:cd06530    3 VVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSpgDPGKPIIKRVIG-------------------------- 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 365233140 108 enkkhkvgeyltenfnskdlkgtngnmkipngkYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKV 171
Cdd:cd06530   57 ---------------------------------YFVLGDNRNNSLDSRY--WGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
21-89 1.56e-05

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 44.27  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  21 LVQKFLFASYTVKGASMHPTFENREKVIVSSIA---------KTLdhIDTG-----DVVIFH--ANAKQDYIKRLIGKPG 84
Cdd:PRK10861  76 IVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAygikdpitqTTL--IETGhpkrgDIVVFKypEDPKLDYIKRVVGLPG 153


                 ....*
gi 365233140  85 DSVEY 89
Cdd:PRK10861 154 DKVTY 158
 
Name Accession Description Interval E-value
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 21-176 6.41e-55

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: 171.62  E-value: 6.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   21 LVQKFLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGKPGDSVEYKKDQLYLNG 98
Cdd:pfam10502  17 LIRTFLFEPYVVPGGSMSPTLPIGDYLIVNKFSYGLGEPKRGDIVVFRPpeGPGVPLIKRVIGLPGDRVEYKDDQLYING 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 365233140   99 KKVDEPYLSENKKHkvgeyltenfNSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKVVLRYW 176
Cdd:pfam10502  97 KPVGEPYLADRKGR----------PTFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRY--FGFVPASNIVGRAVFPVW 162
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 25-179 1.45e-48

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: 154.69  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   25 FLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGKPGDSVEYKKDQLYLNGKKVD 102
Cdd:TIGR02227   1 FVFFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDpdTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 365233140  103 EPYLSENKkhkvgeyltenfnSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKVVLRYWPFN 179
Cdd:TIGR02227  81 EPYLKPNG-------------YLDTSEFNTPVKVPPGHYFVLGDNRDNSLDSRY--FGFVPIDQIIGKVSFVFYPFD 142
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
2-187 2.57e-30

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


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 109.56  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140   2 KKEIIEWIVAIIVAIVIVTLVQKFLFASYTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRL 79
Cdd:COG0681    8 KRELREWLKSIVIALLLALLIRTFVFEPFVIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFKYpeDPSKDYIKRV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  80 IGKPGDSVEYKKDQLYLNGKKVDEPYLsenkkhkvGEYLTENFNSKDLKGTNGNMKIPNGKYLVLGDNRQNSIDSRMDEV 159
Cdd:COG0681   88 IGLPGDTVEIRDGQVYVNGKPLNEPYL--------EEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGV 159

                        170       180
                 ....*....|....*....|....*...
gi 365233140 160 GLLDKNQVVGKVVLRYWPFNRWGGSFNP 187
Cdd:COG0681  160 GVDGVGVGGVVDVVVPDVDSRLVDVGDG 187
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 62-177 7.21e-23

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: 88.04  E-value: 7.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  62 GDVVIFHA-----------NAKQDYIKRLIGKPGDSVEYKKDQLYLNGKKVDEPYLSENKkhkvgeyltenfnSKDLKGT 130
Cdd:COG4959    2 GDLVAFRPpeplaaergylPRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRA-------------GRPLPVW 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 365233140 131 NGNMKIPNGKYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKVVLRYWP 177
Cdd:COG4959   69 QGCGVVPEGEYFLLGDNRPNSFDSRY--FGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 30-171 2.03e-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: 70.69  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  30 YTVKGASMHPTFENREKVIVSSIAKTLDHIDTGDVVIFHA--NAKQDYIKRLIGkpgdsveykkdqlylngkkvdepyls 107
Cdd:cd06530    3 VVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSpgDPGKPIIKRVIG-------------------------- 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 365233140 108 enkkhkvgeyltenfnskdlkgtngnmkipngkYLVLGDNRQNSIDSRMdeVGLLDKNQVVGKV 171
Cdd:cd06530   57 ---------------------------------YFVLGDNRNNSLDSRY--WGPVPEDDIVGKV 85
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 30-115 1.22e-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: 58.04  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  30 YTVKGASMHPTFENREKVIVSsiaKTLDHIDTGDVVIFHANAKQDYIKRLIGKPGdsveykKDQLYL---NGKKVDEPYL 106
Cdd:cd06462    3 LRVEGDSMEPTIPDGDLVLVD---KSSYEPKRGDIVVFRLPGGELTVKRVIGLPG------EGHYFLlgdNPNSPDSRID 73


                 ....*....
gi 365233140 107 SENKKHKVG 115
Cdd:cd06462   74 GPPELDIVG 82
PRK10861 PRK10861
signal peptidase I;
21-89 1.56e-05

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 44.27  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365233140  21 LVQKFLFASYTVKGASMHPTFENREKVIVSSIA---------KTLdhIDTG-----DVVIFH--ANAKQDYIKRLIGKPG 84
Cdd:PRK10861  76 IVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAygikdpitqTTL--IETGhpkrgDIVVFKypEDPKLDYIKRVVGLPG 153


                 ....*
gi 365233140  85 DSVEY 89
Cdd:PRK10861 154 DKVTY 158
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 31-88 6.59e-04

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


Pssm-ID: 442176  Cd Length: 121  Bit Score: 38.02  E-value: 6.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 365233140  31 TVKGASMHPTFENREKVIVSsiaKTLDHIDTGDVVIFHANaKQDYIKRLIGKPGDSVE 88
Cdd:COG2932   39 RVSGDSMEPTIRDGDIVLVD---PSDTEIRDGGIYVVRTD-GELLVKRLQRRPDGKLR 92
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 31-88 1.56e-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: 36.00  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 365233140  31 TVKGASMHPTFENREKVIVssiaKTLDHIDTGDVVIFHaNAKQDYIKRLIGKPGDSVE 88
Cdd:cd06529    4 RVKGDSMEPTIPDGDLVLV----DPSDTPRDGDIVVAR-LDGELTVKRLQRRGGGRLR 56
 
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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