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: 17-Jan-2013
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:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
1Y7O_A        37 DIYSRLLKDRIIXLTGpveDNXANSVIAQLLFLDAQdstkDIYLYVNTPgg---------svSAGLAIVDTXNFi--kAD 105
gi 159470091  44 DLATRLFSERIMYLGMpidSSVAELLTAQLFVLVQEap-dPIFFYINSTgiakst-tkfgneHEAIAVYSMMKGvqkyCP 121
gi 224284163 106 DLPSLLLNSRIIFIGMplvPAVTELVIAEFLYLQWLdprqPTYVYINSTgtsredgetvaleTEGFAIYDTMMQm--kNE 183
gi 168007320  42 DLPSYLFKNRIVFLAMslvPAVTELVMAELLYLQYDdpekSIYMYINSTgttkdg-eklgyeTEAFAIYDTMRYv--kPP 118
gi 81708690   28 DLPSLLLNERIVYLGTpinDVVAELLIAQLLYLESEdnakPIEIYINSPgva-------gfeTSAFAVYDTMRHv--rMP 98
1TYF_A        18 DIYSRLLKERVIFLTGqveDHMANLIVAQMLFLEAEnpekDIYLYINSPgg---------viTAGMSIYDTMQFi--kPD 86
gi 75301253  105 DLASYLFKNRIVYLGMslvPSVTELILAEFLYLQYEdeekPIYLYINSTgttkng-eklgydTEAFAIYDVMGYv--kPP 181
gi 119358788  65 DLPSFIFQERIVYLGMtlvPSVTELILAELLYLQYEdkkkPIQLYINSTgsskdg-kkygydSEAFAIYDTIQYv--sPP 141
gi 168013355  75 DLPSLLLNSRIVYIGMplvPAVTELVIAELLYLQYAdprqPIYVYINSTgtaradgetvgleTEGFAIYDTLMNv--rNQ 152
gi 75301131  121 DLPSMLLDGRIVYIGMplvPAVTELVVAELMYLQWLdpkePIYIYINSTgttrddgetvgmeSEGFAIYDSLMQl--kNE 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                  #                        #                                            
1Y7O_A       106 VQTIVxGXAASXGTVIASSGakgkRFXLPNAEYXIHqPXGGTgggtqqtDMAIAPEHLLKTRNTLEKILAENSGQsxEKV 185
gi 159470091 122 IYTLCvGNAFGEAALLLSAGspgkRAALRSSTIMLRqPLQRLggm-qasDIDIYRKITREKTATMAKYLAACTKKteEQI 200
gi 224284163 184 IHTVAfGAAVGQACLLLAAGkkgkRYMLPHAQVLLQqPRLPAtgqmpaiDVHIRAKELIHNRDTFVKLLAKHTGNpfETV 263
gi 168007320 119 IFTLCvGNAWGEAALLLAAGskgnRACLPSATIMLKqPIAQFrgq--atDIDIARKEVRNVKEELVKLISRHTGQtvEKI 196
gi 81708690   99 IKTIClGLAGGFSALLMAAGtkgqRMSLPNSRIILYqPYGGArgq--atDINIRAQELLTTKRTLNQLLSIHTGKtvEQI 176
1TYF_A        87 VSTICmGQAASMGAFLLTAGakgkRFCLPNSRVMIHqPLGGYqgq--atDIEIHAREILKVKGRMNELMALHTGQslEQI 164
gi 75301253  182 IFTLCvGNAWGEAALLLTAGakgnRSALPSSTIMIKqPIARFqgq--atDVEIARKEIKHIKTEMVKLYSKHIGKspEQI 259
gi 119358788 142 VHTIAvGTAWGEAAMLLASGskgqRAALPSASIMLKqPLSSFrgq--asELEIQRQEMRNTKKQMLDILAKTTGRdiATI 219
gi 168013355 153 IQTVAvGAAIGQACLLLASGdkgmRYMMPHATAMIQqPRLPStgqmsaiDVHIRAKELINNRDTLVGLLAKHTGNpvEKV 232
gi 75301131  199 VHTVCvGAAIGQACLLLSAGtkgkRFMMPHAKAMIQqPRVPSsglmpasDVLIRAKEVITNRDILVELLSKHTGNsvETV 278
                        170       180
                 ....*....|....*....|....
Feature 1              #                 
1Y7O_A       186 HADaeRDNWXSAQETLEYGFIDEI 209
gi 159470091 201 MTDftRPRYFNPYEAVSYGLIDTV 224
gi 224284163 264 AKAmeRPFYMFPRQAVEFGVADKI 287
gi 168007320 197 TDDirRPKYFKPDEAVDYGLIDKV 220
gi 81708690  177 DKDteRLFYMSPQEAVSYGLIDKV 200
1TYF_A       165 ERDteRDRFLSAPEAVEYGLVDSI 188
gi 75301253  260 EADmkRPKYFSPTEAVEYGIIDKV 283
gi 119358788 220 ETDinRPLYFEPSEAIKYGLIDKV 243
gi 168013355 233 AKVmeRPFYMNPKKAVDFGVADKI 256
gi 75301131  279 ANVmrRPYYMDAPKAKEFGVIDRI 302

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