1Y7O,2CBY,2CBY,1TG6,1TYF,2ZL3,2ZL0,2F6I,1YG8,2CE3,2C8T


Conserved Protein Domain Family
S14_ClpP_2

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cd07017: S14_ClpP_2 
Click on image for an interactive view with Cn3D
Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease
Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. They are also implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong to the family of ATP-dependent proteases; the functional Clp protease is comprised of two components: a proteolytic component and one of several regulatory ATPase components, both of which are required for effective levels of protease activity in the presence of ATP, although the proteolytic subunit alone does possess some catalytic activity. Active site consists of the triad Ser, His and Asp; some members have lost all of these active site residues and are therefore inactive, while others may have one or two large insertions. ClpP seems to prefer hydrophobic or non-polar residues at P1 or P1' positions in its substrate. The protease exists as a tetradecamer made up of two heptameric rings stacked back-to-back such that the catalytic triad of each subunit is located at the interface between three monomers, thus making oligomerization essential for function.
Statistics
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PSSM-Id: 132928
View PSSM: cd07017
Aligned: 189 rows
Threshold Bit Score: 106.372
Threshold Setting Gi: 193875742
Created: 25-Nov-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active siteoligomer
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:active site residues [active site]
Evidence:
  • Comment:The catalytic triad is in the order Ser, His, Asp, which is an arrangement not seen in peptidases of any other family.
  • Structure:1TYF: E. coli Clp protease (ClpP)
    View structure with Cn3D
  • Citation:PMID 9390554

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                        
1Y7O_A        37 DIYSRLLKDRIIXLTGpveDNXANSVIAQLLFLDAQdstkDIYLYVNTPgg---------svSAGLAIVDTXNFi--kAD 105 Streptococcus p...
XP_001693193  44 DLATRLFSERIMYLGMpidSSVAELLTAQLFVLVQEap-dPIFFYINSTgiakst-tkfgneHEAIAVYSMMKGvqkyCP 121 Chlamydomonas r...
ACN39818     106 DLPSLLLNSRIIFIGMplvPAVTELVIAEFLYLQWLdprqPTYVYINSTgtsredgetvaleTEGFAIYDTMMQm--kNE 183 Sitka spruce
XP_001756356  42 DLPSYLFKNRIVFLAMslvPAVTELVMAELLYLQYDdpekSIYMYINSTgttkdg-eklgyeTEAFAIYDTMRYv--kPP 118 Physcomitrella ...
Q7NEW1        28 DLPSLLLNERIVYLGTpinDVVAELLIAQLLYLESEdnakPIEIYINSPgva-------gfeTSAFAVYDTMRHv--rMP 98  Gloeobacter vio...
1TYF_A        18 DIYSRLLKERVIFLTGqveDHMANLIVAQMLFLEAEnpekDIYLYINSPgg---------viTAGMSIYDTMQFi--kPD 86  Escherichia coli
Q8LB10       105 DLASYLFKNRIVYLGMslvPSVTELILAEFLYLQYEdeekPIYLYINSTgttkng-eklgydTEAFAIYDVMGYv--kPP 181 thale cress
CAL52028      65 DLPSFIFQERIVYLGMtlvPSVTELILAELLYLQYEdkkkPIQLYINSTgsskdg-kkygydSEAFAIYDTIQYv--sPP 141 Ostreococcus tauri
XP_001759365  75 DLPSLLLNSRIVYIGMplvPAVTELVIAELLYLQYAdprqPIYVYINSTgtaradgetvgleTEGFAIYDTLMNv--rNQ 152 Physcomitrella ...
Q8L770       121 DLPSMLLDGRIVYIGMplvPAVTELVVAELMYLQWLdpkePIYIYINSTgttrddgetvgmeSEGFAIYDSLMQl--kNE 198 thale cress
Feature 1                  #                        #                                            
1Y7O_A       106 VQTIVxGXAASXGTVIASSGakgkRFXLPNAEYXIHqPXGGTgggtqqtDMAIAPEHLLKTRNTLEKILAENSGQsxEKV 185 Streptococcus p...
XP_001693193 122 IYTLCvGNAFGEAALLLSAGspgkRAALRSSTIMLRqPLQRLggm-qasDIDIYRKITREKTATMAKYLAACTKKteEQI 200 Chlamydomonas r...
ACN39818     184 IHTVAfGAAVGQACLLLAAGkkgkRYMLPHAQVLLQqPRLPAtgqmpaiDVHIRAKELIHNRDTFVKLLAKHTGNpfETV 263 Sitka spruce
XP_001756356 119 IFTLCvGNAWGEAALLLAAGskgnRACLPSATIMLKqPIAQFrgq--atDIDIARKEVRNVKEELVKLISRHTGQtvEKI 196 Physcomitrella ...
Q7NEW1        99 IKTIClGLAGGFSALLMAAGtkgqRMSLPNSRIILYqPYGGArgq--atDINIRAQELLTTKRTLNQLLSIHTGKtvEQI 176 Gloeobacter vio...
1TYF_A        87 VSTICmGQAASMGAFLLTAGakgkRFCLPNSRVMIHqPLGGYqgq--atDIEIHAREILKVKGRMNELMALHTGQslEQI 164 Escherichia coli
Q8LB10       182 IFTLCvGNAWGEAALLLTAGakgnRSALPSSTIMIKqPIARFqgq--atDVEIARKEIKHIKTEMVKLYSKHIGKspEQI 259 thale cress
CAL52028     142 VHTIAvGTAWGEAAMLLASGskgqRAALPSASIMLKqPLSSFrgq--asELEIQRQEMRNTKKQMLDILAKTTGRdiATI 219 Ostreococcus tauri
XP_001759365 153 IQTVAvGAAIGQACLLLASGdkgmRYMMPHATAMIQqPRLPStgqmsaiDVHIRAKELINNRDTLVGLLAKHTGNpvEKV 232 Physcomitrella ...
Q8L770       199 VHTVCvGAAIGQACLLLSAGtkgkRFMMPHAKAMIQqPRVPSsglmpasDVLIRAKEVITNRDILVELLSKHTGNsvETV 278 thale cress
Feature 1              #                 
1Y7O_A       186 HADaeRDNWXSAQETLEYGFIDEI 209 Streptococcus pneumoniae
XP_001693193 201 MTDftRPRYFNPYEAVSYGLIDTV 224 Chlamydomonas reinhardtii
ACN39818     264 AKAmeRPFYMFPRQAVEFGVADKI 287 Sitka spruce
XP_001756356 197 TDDirRPKYFKPDEAVDYGLIDKV 220 Physcomitrella patens subsp. patens
Q7NEW1       177 DKDteRLFYMSPQEAVSYGLIDKV 200 Gloeobacter violaceus
1TYF_A       165 ERDteRDRFLSAPEAVEYGLVDSI 188 Escherichia coli
Q8LB10       260 EADmkRPKYFSPTEAVEYGIIDKV 283 thale cress
CAL52028     220 ETDinRPLYFEPSEAIKYGLIDKV 243 Ostreococcus tauri
XP_001759365 233 AKVmeRPFYMNPKKAVDFGVADKI 256 Physcomitrella patens subsp. patens
Q8L770       279 ANVmrRPYYMDAPKAKEFGVIDRI 302 thale cress

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