1T7D,1B12,1KN9


Conserved Protein Domain Family
S26_SPase_I

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cd06530: S26_SPase_I 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 119398
View PSSM: cd06530
Aligned: 377 rows
Threshold Bit Score: 37.5651
Threshold Setting Gi: 166032689
Created: 25-Jul-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Catalytic site
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:Catalytic site [active site]
Evidence:
  • Comment:These serine proteases carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.
  • Structure:1T7D: Lipopeptide inhibitor arylomycin A2 blocks the active site of Escherichia coli type I signal peptidase
    View structure with Cn3D
  • Structure:1B12: A beta-lactam inhibitor, (5S,6S)-penem, blocks the active site of Escherichia coli type I signal peptidase
    View structure with Cn3D
  • Citation:PMID 982390

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                #                                                               #       
1T7D_A         9 EPFQIPSGSMmptllIGDFILVEkfaygikdpiyqktlietghpkrGDIVVFKYped---------pklDYIKRAVGlpg 79  Escherichia coli
YP_174253     45 TSYTILSNSMeptfsAGDVVIMKknee----------------psiGDVVTFMApe-----------rrLFTHRIVEkfe 97  Bacillus clausi...
YP_291017    110 QALIVLSGSMepalpVGSVVIAGpveph--------------eidvGDIITFTHadpaqtevantttlpLVTHRVIDiet 175 Thermobifida fu...
ZP_01129385   57 TPLTVLTSSMepglpPGTLVVVKpidpn--------------eiamGDVITYQIesg---------kpgVITHRVTGvtn 113 marine actinoba...
YP_925421     42 TPFAVLTGSMrpvmpPGTLVVVRpvdpa--------------didvGSVITFMPreh---------dpaVVTHRVVGvgf 98  Nocardioides sp...
YP_001221988  74 VPLTILTQSMeptlpPGTLIVVRpvdpd--------------aleiGDVATYQIrsg---------dpaVITHRITAias 130 Clavibacter mic...
ZP_02016102   42 ESFVVLTPSMtpeiaPGDVVIVAerdpt--------------aiveGDVITFARgas----------dvPVTHRVIDvvd 97  Halorubrum lacu...
YP_001626115  57 ETFTVLTGSMrpglqPGDLLVIKatpve--------------nisiGSVVSYQLnsg---------lsdVVTHRVVGisv 113 Renibacterium s...
ZP_02836601   66 QTSTMLTGSMsplinPGDVVVSVptpvt--------------dlkvGDIVTYHIpve---------dqrIETHRVTDvtr 122 Arthrobacter ch...
YP_001711436  65 RFVPVLSDSMapgmpVGSLAITAptpra--------------evatGDVVVFTApsg---------prvRVIHRVTHvfg 121 Clavibacter mic...
Feature 1                                                                                        
1T7D_A        80 dkvtydpvskeltiqpgcssgqacenalpvtysnvepsdfvqtfsrrnggeatsgffevpknetkengirlserketlgd 159 Escherichia coli
YP_174253     98 sn------------------------------------------------------------------------------ 99  Bacillus clausi...
YP_291017    176 te------------------------------------------------------------------------------ 177 Thermobifida fu...
ZP_01129385  114 ss------------------------------------------------------------------------------ 115 marine actinoba...
YP_925421     99 da------------------------------------------------------------------------------ 100 Nocardioides sp...
YP_001221988 131 as------------------------------------------------------------------------------ 132 Clavibacter mic...
ZP_02016102   98 eg------------------------------------------------------------------------------ 99  Halorubrum lacu...
YP_001626115 114 ap------------------------------------------------------------------------------ 115 Renibacterium s...
ZP_02836601  123 ag------------------------------------------------------------------------------ 124 Arthrobacter ch...
YP_001711436 122 pedaerl------------------------------------------------------------------------- 128 Clavibacter mic...
Feature 1                                                                                        
1T7D_A       160 vthriltvpiaqdqvgmyyqqpgqqlatwivppgqYFMMGDnrdNSADSRYWgfv------------------------- 214 Escherichia coli
YP_174253    100 -------------------------------gktyYKTQGDn-nNVVDEDPIv--------------------------- 120 Bacillus clausi...
YP_291017    178 -------------------------------egivFHTQGDa--NTVPDEPPvp-------------------------- 198 Thermobifida fu...
ZP_01129385  116 ------------------------------dgsrtFTLQGDn--NDVADELQvl-------------------------- 137 marine actinoba...
YP_925421    101 ------------------------------tgqpaFRTKGDa--NDAPDGAMvr-------------------------- 122 Nocardioides sp...
YP_001221988 133 ------------------------------dgtrsFTFKGDn--NASPDSLPvt-------------------------- 154 Clavibacter mic...
ZP_02016102  100 -------------------------------gglaFETQGDa--NEGPDPGLvp-------------------------- 120 Halorubrum lacu...
YP_001626115 116 ------------------------------ngernFQMQGDa--NNTPDAAAvr-------------------------- 137 Renibacterium s...
ZP_02836601  125 -------------------------------asttIQTKGDa--NNGADPWNatmaddhafttva--------viphlgd 163 Arthrobacter ch...
YP_001711436 129 --------------------------dgwsddrlaIQTKGDn--NPSGDPWIvtigddavwertsvvpflgwpfvwlgdp 180 Clavibacter mic...
Feature 1                     
1T7D_A       215 ----peANLVGRA 223 Escherichia coli
YP_174253    121 -----kEQIVGTH 128 Bacillus clausii KSM-K16
YP_291017    199 -----aADVRGKV 206 Thermobifida fusca YX
ZP_01129385  138 -----pIQVVGKL 145 marine actinobacterium PHSC20C1
YP_925421    123 -----tYQIVGER 130 Nocardioides sp. JS614
YP_001221988 155 -----pGQIQGEV 162 Clavibacter michiganensis subsp. michiganensis NCPPB 382
ZP_02016102  121 -----aANLVGAV 128 Halorubrum lacusprofundi ATCC 49239
YP_001626115 138 -----pVQIRGVL 145 Renibacterium salmoninarum ATCC 33209
ZP_02836601  164 airalrSPVVGKV 176 Arthrobacter chlorophenolicus A6
YP_001711436 181 itraiaFAVVGAV 193 Clavibacter michiganensis subsp. sepedonicus

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