1TYF,1Y7O


Conserved Protein Domain Family
S14_ClpP

?
cd07013: S14_ClpP 
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. Additionally, they are 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
?
PSSM-Id: 132924
View PSSM: cd07013
Aligned: 3 rows
Threshold Bit Score: 232.157
Threshold Setting Gi: 61680536
Created: 21-Nov-2008
Updated: 17-Jan-2013
Structure
?
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
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                #       
1TYF_A        27 RVIFLTGqve--dhmANLIVAQMLFLEAenpekDIYLYINSPggviTAGMSIYDTMQFikPDVSTICmGQAASMGAFLLT 104
1Y7O_A        46 RIIXLTGpve--dnxANSVIAQLLFLDAqdstkDIYLYVNTPggsvSAGLAIVDTXNFikADVQTIVxGXAASXGTVIAS 123
gi 160873909  26 AELMIYDeiggwgisAQQFARDLQALGKv---gTITARIHSPggdvFEGMAIYNMIKGhpAHKVCYIdGLAASMASVIAM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                          #                                                  #          
1TYF_A       105 AGakgkRFCLP-NSRVMIHqPLGGYqgq--atDIEIHAREILKVKGRMNELMALHTGqslEQIERDterDRFLSAPEAVE 181
1Y7O_A       124 SGakgkRFXLP-NAEYXIHqPXGGTgggtqqtDMAIAPEHLLKTRNTLEKILAENSGqsxEKVHADaerDNWXSAQETLE 202
gi 160873909 103 AFd---EVIMPeNAMMMVHkPWGGTlgd--aeDMRKYADLLDKVEGNLVSAYQHKTGlseDELHALlaaETWLTGREAVE 177

                 ....*..
Feature 1               
1TYF_A       182 YGLVDSI 188
1Y7O_A       203 YGFIDEI 209
gi 160873909 178 KGFANTL 184

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap