Clp Protease: Difference between revisions

Revision as of 12:21, 5 December 2013

E. coli Clp protease, 1tyf

Activity:

Endopeptidase Clp, with EC number 3.4.21.92

Structural annotation:
Resources:	CATH : 1Tyfa00, 1Tyfb00, 1Tyfc00, 1Tyfd00, 1Tyfe00, 1Tyff00, 1Tyfg00, 1Tyfh00, 1Tyfi00, 1Tyfj00, 1Tyfk00, 1Tyfl00, 1Tyfm00, 1Tyfn00 InterPro : Ipr001907 Pfam : PF00574 SCOP : d1tyfa_, d1tyfb_, d1tyfc_, d1tyfd_, d1tyfe_, d1tyff_, d1tyfg_, d1tyfh_, d1tyfi_, d1tyfj_, d1tyfk_, d1tyfl_, d1tyfm_, d1tyfn_ UniProt : P0A6G7

Functional annotation:
Cellular component:	cytoplasm membrane fraction
Biological process:	response to stress proteolysis
Molecular function:	endopeptidase Clp activity serine-type endopeptidase activity peptidase activity hydrolase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Clp protease (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion. CLP is found in mitochondria. CLP participates in degradation of misfolded proteins. CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P. For more details see Clp protease.

3D structures of Clp protease3D structures of Clp protease

Updated on 05-December-2013

CLP P subunitCLP P subunit

1tyf, 1yg6 – EcCLP – Escherichia coli
1yg8, 3hln - EcCLP (mutant)
1y7o – CLP – Streptococcus pneumoniae
1tg6 - CLP – human
2f6i, 4gm2, 4hnk - CLP – Plasmodium falciparum
2cby, 2ce3, 2c8t - CLP – Mycobacterium tuberculosis
3fes - CLP – Clostridium difficile
3ktg, 3kth, 3tt6 – BsCLP – Bacillus subtilis
3p2l - CLP – Francisella tulerensis
3q7h - CLP – Coxiella burnetii
3qwd, 3st9, 3sta, 3v5e, 4emm - SaCLP – Staphylococcus aureus
3v5i, 4emp - SaCLP (mutant)
2zl0 - HpCLP – Helicobacter pylori
2zl3 - HpCLP (mutant)

CLP P subunit binary complex

2fzs, 3mt6 - EcCLP + peptide
2zl2 - HpCLP + peptide
2zl4 - HpCLP (mutant) + peptide
3kti, 3ktj, 3ktk - BsCLP + peptide
3tt7 - BsCLP + DFP

CLP A subunitCLP A subunit

1k6k, 1r6c – EcCLP N terminal
1ovx - EcCLP N terminal - NMR
1ksf, 1r6b – EcCLP (mutant)
1um8 – HpCLP

CLP A subunit binary complex

1lzw, 1mg9, 1mbu, 1mbv, 1mbx – EcCLP + CLP adaptor protein ClpS
1r6o, 1r6q - EcCLP N terminal + CLP adaptor protein ClpS

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1tyf|  PDB=1tyf  | SIZE=400| SCENE= |right|CAPTION=Clp protease A subunit complex with peptide, [[1tyf]] }}
+{{STRUCTURE_1tyf|  PDB=1tyf  | SIZE=400| SCENE= |right|CAPTION=E. coli Clp protease, [[1tyf]] }}
-{{STRUCTURE_2zl2|  PDB=2zl2  | SIZE=400| SCENE= |right|CAPTION=Clp protease A subunit complex with peptide, [[2zl2]] }}
 '''Clp protease''' (CLP) is a serine peptidase which hydrolyzes proteins in the presence of ATP and Mg+2 ion.  CLP is found in mitochondria.  CLP participates in degradation of misfolded proteins.  CLP is a heterodimer containing an ATP-binding regulatory subunit A and catalytic subunit P.  For more details see [[Clp protease]].