ATP-dependent Clp protease proteolytic subunit

Details

Name
ATP-dependent Clp protease proteolytic subunit
Synonyms
  • 3.4.21.92
  • Caseinolytic protease
  • Endopeptidase Clp
  • Heat shock protein F21.5
  • lopP
  • Protease Ti
Gene Name
clpP
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012791|ATP-dependent Clp protease proteolytic subunit
MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQ
MLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAG
AKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIER
DTERDRFLSAPEAVEYGLVDSILTHRN
Number of residues
207
Molecular Weight
23186.46
Theoretical pI
5.61
GO Classification
Functions
ATP-dependent peptidase activity / identical protein binding / serine-type endopeptidase activity / serine-type peptidase activity
Processes
misfolded or incompletely synthesized protein catabolic process / proteasomal protein catabolic process / response to heat / response to temperature stimulus
Components
cytosol / membrane
General Function
Serine-type peptidase activity
Specific Function
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE (PubMed:24375411).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012792|ATP-dependent Clp protease proteolytic subunit (clpP)
ATGTCATACAGCGGCGAACGAGATAACTTTGCACCCCATATGGCGCTGGTGCCGATGGTC
ATTGAACAGACCTCACGCGGTGAGCGCTCTTTTGATATCTATTCTCGTCTACTTAAGGAA
CGCGTCATTTTTCTGACTGGCCAGGTTGAAGACCACATGGCTAACCTGATTGTGGCGCAG
ATGCTGTTCCTGGAAGCGGAAAACCCAGAAAAAGATATCTATCTGTACATTAACTCCCCA
GGCGGGGTGATCACTGCCGGGATGTCTATCTATGACACCATGCAGTTTATCAAGCCTGAT
GTCAGCACCATCTGTATGGGCCAGGCGGCCTCGATGGGCGCTTTCTTGCTGACCGCAGGG
GCAAAAGGTAAACGTTTTTGCCTGCCGAATTCGCGCGTGATGATTCACCAACCGTTGGGC
GGCTACCAGGGCCAGGCGACCGATATCGAAATTCATGCCCGTGAAATTCTGAAAGTTAAA
GGGCGCATGAATGAACTTATGGCGCTTCATACGGGTCAATCATTAGAACAGATTGAACGT
GATACCGAGCGCGATCGCTTCCTTTCCGCCCCTGAAGCGGTGGAATACGGTCTGGTCGAT
TCGATTCTGACCCATCGTAATTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A6G7
UniProtKB Entry NameCLPP_ECOLI
GenBank Protein ID145555
GenBank Gene IDJ05534
General References
  1. Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S: Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J Biol Chem. 1990 Jul 25;265(21):12536-45. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Kroh HE, Simon LD: The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. J Bacteriol. 1990 Oct;172(10):6026-34. [Article]
  5. Arribas J, Castano JG: A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. J Biol Chem. 1993 Oct 5;268(28):21165-71. [Article]
  6. Yoo SJ, Seol JH, Kang MS, Ha DB, Chung CH: clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can be expressed independently from clpP in Escherichia coli. Biochem Biophys Res Commun. 1994 Sep 15;203(2):798-804. [Article]
  7. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  8. Kenniston JA, Baker TA, Fernandez JM, Sauer RT: Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell. 2003 Aug 22;114(4):511-20. [Article]
  9. Flynn JM, Levchenko I, Sauer RT, Baker TA: Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev. 2004 Sep 15;18(18):2292-301. [Article]
  10. Erental A, Sharon I, Engelberg-Kulka H: Two programmed cell death systems in Escherichia coli: an apoptotic-like death is inhibited by the mazEF-mediated death pathway. PLoS Biol. 2012;10(3):e1001281. doi: 10.1371/journal.pbio.1001281. Epub 2012 Mar 6. [Article]
  11. Tripathi A, Dewan PC, Siddique SA, Varadarajan R: MazF-induced growth inhibition and persister generation in Escherichia coli. J Biol Chem. 2014 Feb 14;289(7):4191-205. doi: 10.1074/jbc.M113.510511. Epub 2013 Dec 27. [Article]
  12. Shin DH, Lee CS, Chung CH, Suh SW: Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome. J Mol Biol. 1996 Sep 20;262(2):71-6. [Article]
  13. Wang J, Hartling JA, Flanagan JM: The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell. 1997 Nov 14;91(4):447-56. [Article]
  14. Bewley MC, Graziano V, Griffin K, Flanagan JM: The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes. J Struct Biol. 2006 Feb;153(2):113-28. Epub 2005 Dec 1. [Article]
  15. Szyk A, Maurizi MR: Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site. J Struct Biol. 2006 Oct;156(1):165-74. Epub 2006 Apr 21. [Article]
  16. Li DH, Chung YS, Gloyd M, Joseph E, Ghirlando R, Wright GD, Cheng YQ, Maurizi MR, Guarne A, Ortega J: Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP. Chem Biol. 2010 Sep 24;17(9):959-69. doi: 10.1016/j.chembiol.2010.07.008. [Article]
  17. Kimber MS, Yu AY, Borg M, Leung E, Chan HS, Houry WA: Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure. 2010 Jul 14;18(7):798-808. doi: 10.1016/j.str.2010.04.008. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07571N~2~-[(BENZYLOXY)CARBONYL]-N-[(1S,2S)-2-HYDROXY-1-(4-HYDROXYBENZYL)PROPYL]-L-LEUCINAMIDEexperimentalunknownDetails