Conserved Protein Domain Family
S14_ClpP_1

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cd07016: S14_ClpP_1 
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. This subfamily only contains bacterial sequences. 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: 132927
View PSSM: cd07016
Aligned: 111 rows
Threshold Bit Score: 108.391
Threshold Setting Gi: 110633689
Created: 25-Nov-2008
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
active siteoligomer
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.
  • Citation:PMID 9390554

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                        
YP_001553225  26 AELMIYDEIggw----gisAQQFARDLQALGKv----GTITARIHSPGGDVFEGMAIYNMIKGh-----pAHKVCYIDGL 92  Shewanella balt...
ZP_03011816   37 STIFLYGDIgdyt---evqSGRIAQELMEAERv---sRRIHVRINSNGGEVYSGIAIFNALRHs-----qADIRIYVDGI 105 Bacteroides cop...
ZP_01694334   17 AHILLYDKIgvdeegkgisGRRFAEELFRLTKr---fRRINVRINSPGGKITDGLSICAAILNinqstpnVRIDTYVDGL 93  Microscilla mar...
ZP_02071238    4 TVITLFGTIdry----wynKNYLKYFLDKAKG-----QPVRLKVSSYGGDVAEAVAMSALMAEh------GNVTVEFISF 68  Bacteroides uni...
ZP_02426000   67 PEEWQFDQPssr----vatYEKFRDSLDRLREid--aPEIVVNIRSTGGDVNDALLIYEALSSl-----dGHIVTRCYGY 135 Alistipes putre...
ZP_03643686   19 AVIRFFGRVte------etTSRFNDEFDFLENii-rpSCIRVLINSEGGSVLYGMSTYSTIANa-----tVDTECIIEGV 86  Bacteroides cop...
YP_673897     41 AKVFFVGEVte------rkVAELVSVLDRLNSehkalQSIYLYINSPGGDMDSAQAAYWAIKSs-----pIPVIAVNIST 109 Mesorhizobium s...
ZP_02426428   19 ASIRFFGRIte------esAGRFSEAFDFLENiv-rpSLIRVLINSEGGSVLHGMTVYAAIQNa-----sVPTECVIEGM 86  Alistipes putre...
ZP_03699702   35 SEISFYLCGei------qaSHFYTNLFYTLRSas-etDIIYLHLNTTGGDFDTGMQIINNMQSs-----cAHVITVLEAR 102 Chromobacterium...
NP_900815     28 RQISFYLSEei------gaAIHYTDLLYTLRTas-stDIVYLHLNTPGGNFDAGLQIINNITAs-----qAHVVTILEAR 95  Chromobacterium...
Feature 1          #                         #                                                   
YP_001553225  93 AASMASVIAMAFD---EVIMPeNAMMMVHKPWGGTlgd-----------aeDMRKYADLLDKVEGNLVSAYQHKTGlseD 158 Shewanella balt...
ZP_03011816  106 AASMASVIALCGK---PVEMSkYARLMLHSVSGGCygn-----------kqDLQRCMEEIESLEGSLSEIYAERLGmskE 171 Bacteroides cop...
ZP_01694334   94 ALSIAGLIAVCGK---KVGMCnFAKLMLHNPFIGGkng----------tqnGGIEQHETLMQVKEMLLTLLATRTGqkvE 160 Microscilla mar...
ZP_02071238   69 NASAATVLAFGAK---SIEMHeDGMWLAHKCSLGVdiwgqlnadqledtikELQNKKKSAEAIDLMIAQKYINRSGkslK 145 Bacteroides uni...
ZP_02426000  136 TASAATVIAQAASegcREISA-HALYLIHNSICTAegn-----------aeELATRIDLLRKTDARLAEVYAARSGrtpE 203 Alistipes putre...
ZP_03643686   87 AASMASIIWAAGK---RSLMRdYAILMIHNPMLPDddg-----------gePSDMVTAFTKQIETIYRKRFGLKAEh-vR 151 Bacteroides cop...
YP_673897    110 VASVAAVMFCGAAe--RAAFP-NTYFILKPASVTLpems--------mqpvHFELSRELLKSYNEVFESVYRECTSlsaD 178 Mesorhizobium s...
ZP_02426428   87 AASMGSVIWAAGD---KSFMRdYGILMIHNPFLPDend-----------gePSELVKAFTAQIETIYRKRFGLSHEk-vR 151 Alistipes putre...
ZP_03699702  103 AYSMGALIFLAGD---ELEVQdNCQLMFHIYSGTFagr-----------gtEQQAQIQAVSSWFEKVMQRICQPFLs-tA 167 Chromobacterium...
NP_900815     96 AYSMGALIFLAGD---ELVVHdTCQLMFHNYSSALigk-----------gnEQQAQVAASGKWFEKVMRHVCRPFLt-dE 160 Chromobacterium...
Feature 1                    #                    
YP_001553225 159 ELHALLAa----ETWLTG--REAVEKGF-ANTL 184 Shewanella baltica OS195
ZP_03011816  172 EVKQTYFdg--eDHWLTA--KEALDLGF-IDDI 199 Bacteroides coprocola DSM 17136
ZP_01694334  161 DLSLMMNq----TTWLSA--AEAKRQGF-VDEV 186 Microscilla marina ATCC 23134
ZP_02071238  146 DIITLMEe----ERWMPA--AEAKEWGF-IDKI 171 Bacteroides uniformis ATCC 8492
ZP_02426000  204 EFTLLMAenngsGRWLSP--QEALAAGL-VDRI 233 Alistipes putredinis DSM 17216
ZP_03643686  152 AIMDGQAgk--dGTYFDA--QAAVKAGI-IPAE 179 Bacteroides coprophilus DSM 18228
YP_673897    179 EISAVIEs---eDNRLLVraSEAREKGI-ISSE 207 Mesorhizobium sp. BNC1
ZP_02426428  152 AIMDGAAgq--dGTFFDA--AAAVKAGI-IPES 179 Alistipes putredinis DSM 17216
ZP_03699702  168 EVDKVLKg---aDVWMDS--DEIRRRLSrLQRA 195 Chromobacterium sp. 2002
NP_900815    161 ELDRILKg---eDIWLDS--DGIRRRLNnIQKG 188 Chromobacterium violaceum ATCC 12472

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