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ClpP from Neisseria meningitidis - Compressed conformation

Source organism: Neisseria meningitidis
Biochemical function: ATPase binding
Biological process: protein quality control for misfolded or incompletely synthesized proteins
Cellular component: endopeptidase Clp complex

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EC 3.4.21.92: Endopeptidase Clp

Reaction catalysed:
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Systematic name:
-
Alternative Name(s):
  • ATP-dependent Clp protease
  • Caseinolytic protease
  • Clp protease
  • ClpP
  • Endopeptidase Ti
  • Protease Ti

GO terms

Sequence family

Pfam Protein family (Pfam)
PF00574
Domain description: Clp protease
Occurring in:
  1. ATP-dependent Clp protease proteolytic subunit
The deposited structure of PDB entry 7kr2 contains 14 copies of Pfam domain PF00574 (Clp protease) in ATP-dependent Clp protease proteolytic subunit. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR001907
Domain description: ATP-dependent Clp protease proteolytic subunit
Occurring in:
  1. ATP-dependent Clp protease proteolytic subunit
IPR023562
Domain description: Clp protease proteolytic subunit /Translocation-enhancing protein TepA
Occurring in:
  1. ATP-dependent Clp protease proteolytic subunit
IPR033135
Domain description: ClpP, histidine active site
Occurring in:
  1. ATP-dependent Clp protease proteolytic subunit
IPR018215
Domain description: ClpP, Ser active site
Occurring in:
  1. ATP-dependent Clp protease proteolytic subunit
IPR029045
Domain description: ClpP/crotonase-like domain superfamily
Occurring in:
  1. ATP-dependent Clp protease proteolytic subunit

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