ID   CLPP_ECOLI              Reviewed;         207 AA.
AC   P0A6G7; P19245; Q2MBY9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE            EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Caseinolytic protease;
DE   AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Heat shock protein F21.5;
DE   AltName: Full=Protease Ti;
DE   Flags: Precursor;
GN   Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=lopP;
GN   OrderedLocusNames=b0437, JW0427;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 15-36.
RX   PubMed=2197275; DOI=10.1016/s0021-9258(19)38378-4;
RA   Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B.,
RA   Gottesman S.;
RT   "Sequence and structure of Clp P, the proteolytic component of the ATP-
RT   dependent Clp protease of Escherichia coli.";
RL   J. Biol. Chem. 265:12536-12545(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   IDENTIFICATION AS A HEAT SHOCK PROTEIN.
RX   PubMed=2211522; DOI=10.1128/jb.172.10.6026-6034.1990;
RA   Kroh H.E., Simon L.D.;
RT   "The ClpP component of Clp protease is the sigma 32-dependent heat shock
RT   protein F21.5.";
RL   J. Bacteriol. 172:6026-6034(1990).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=8407953; DOI=10.1016/s0021-9258(19)36906-6;
RA   Arribas J., Castano J.G.;
RT   "A comparative study of the chymotrypsin-like activity of the rat liver
RT   multicatalytic proteinase and the ClpP from Escherichia coli.";
RL   J. Biol. Chem. 268:21165-21171(1993).
RN   [7]
RP   INDUCTION, AND OPERON.
RX   PubMed=8093059; DOI=10.1006/bbrc.1994.2253;
RA   Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.;
RT   "clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can
RT   be expressed independently from clpP in Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 203:798-804(1994).
RN   [8]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [9]
RP   FUNCTION.
RX   PubMed=12941278; DOI=10.1016/s0092-8674(03)00612-3;
RA   Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.;
RT   "Linkage between ATP consumption and mechanical unfolding during the
RT   protein processing reactions of an AAA+ degradation machine.";
RL   Cell 114:511-520(2003).
RN   [10]
RP   FUNCTION, AND SUBSTRATE.
RX   PubMed=15371343; DOI=10.1101/gad.1240104;
RA   Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
RT   "Modulating substrate choice: the SspB adaptor delivers a regulator of the
RT   extracytoplasmic-stress response to the AAA+ protease ClpXP for
RT   degradation.";
RL   Genes Dev. 18:2292-2301(2004).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=22412352; DOI=10.1371/journal.pbio.1001281;
RA   Erental A., Sharon I., Engelberg-Kulka H.;
RT   "Two programmed cell death systems in Escherichia coli: an apoptotic-like
RT   death is inhibited by the mazEF-mediated death pathway.";
RL   PLoS Biol. 10:E1001281-E1001281(2012).
RN   [12]
RP   CLEAVAGE OF ANTITOXIN MAZE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113, and K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=24375411; DOI=10.1074/jbc.m113.510511;
RA   Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.;
RT   "MazF-induced growth inhibition and persister generation in Escherichia
RT   coli.";
RL   J. Biol. Chem. 289:4191-4205(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=8831780; DOI=10.1006/jmbi.1996.0499;
RA   Shin D.H., Lee C.S., Chung C.H., Suh S.W.;
RT   "Molecular symmetry of the ClpP component of the ATP-dependent Clp
RT   protease, an Escherichia coli homolog of 20 S proteasome.";
RL   J. Mol. Biol. 262:71-76(1996).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 15-207, AND SUBUNIT.
RX   PubMed=9390554; DOI=10.1016/s0092-8674(00)80431-6;
RA   Wang J., Hartling J.A., Flanagan J.M.;
RT   "The structure of ClpP at 2.3-A resolution suggests a model for ATP-
RT   dependent proteolysis.";
RL   Cell 91:447-456(1997).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, DOMAIN, AND MUTAGENESIS OF VAL-17; PRO-18; MET-19;
RP   VAL-20; ILE-21; THR-24; GLY-27; ASP-32; ILE-33; TYR-34; PHE-126 AND
RP   ASP-185.
RX   PubMed=16406682; DOI=10.1016/j.jsb.2005.09.011;
RA   Bewley M.C., Graziano V., Griffin K., Flanagan J.M.;
RT   "The asymmetry in the mature amino-terminus of ClpP facilitates a local
RT   symmetry match in ClpAP and ClpXP complexes.";
RL   J. Struct. Biol. 153:113-128(2006).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207 BOUND TO INHIBITOR,
RP   ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=16682229; DOI=10.1016/j.jsb.2006.03.013;
RA   Szyk A., Maurizi M.R.;
RT   "Crystal structure at 1.9 A of E. coli ClpP with a peptide covalently bound
RT   at the active site.";
RL   J. Struct. Biol. 156:165-174(2006).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ANTIBIOTIC, AND
RP   SUBUNIT.
RX   PubMed=20851345; DOI=10.1016/j.chembiol.2010.07.008;
RA   Li D.H., Chung Y.S., Gloyd M., Joseph E., Ghirlando R., Wright G.D.,
RA   Cheng Y.Q., Maurizi M.R., Guarne A., Ortega J.;
RT   "Acyldepsipeptide antibiotics induce the formation of a structured axial
RT   channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.";
RL   Chem. Biol. 17:959-969(2010).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=20637416; DOI=10.1016/j.str.2010.04.008;
RA   Kimber M.S., Yu A.Y., Borg M., Leung E., Chan H.S., Houry W.A.;
RT   "Structural and theoretical studies indicate that the cylindrical protease
RT   ClpP samples extended and compact conformations.";
RL   Structure 18:798-808(2010).
CC   -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC       requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC       major role in the degradation of misfolded proteins. May play the role
CC       of a master protease which is attracted to different substrates by
CC       different specificity factors such as ClpA or ClpX. Participates in the
CC       final steps of RseA-sigma-E degradation, liberating sigma-E to induce
CC       the extracytoplasmic-stress response. Degrades antitoxin MazE
CC       (PubMed:24375411). {ECO:0000255|HAMAP-Rule:MF_00444,
CC       ECO:0000269|PubMed:12941278, ECO:0000269|PubMed:15371343,
CC       ECO:0000269|PubMed:24375411}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins to small peptides in the presence of
CC         ATP and magnesium. alpha-casein is the usual test substrate. In the
CC         absence of ATP, only oligopeptides shorter than five residues are
CC         hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC         Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC         occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC   -!- ACTIVITY REGULATION: Inhibited by benzyloxycarbonyl leucyltyrosine
CC       chloromethylketone (Z-LY-CMK). {ECO:0000269|PubMed:16682229}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin
CC         (N-succinyl-Leu-Tyr-AMC) {ECO:0000269|PubMed:16406682,
CC         ECO:0000269|PubMed:20637416};
CC         KM=1 mM for N-succinyl-Leu-Tyr-AMC {ECO:0000269|PubMed:16406682,
CC         ECO:0000269|PubMed:20637416};
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC       stack back to back to give a disk-like structure with a central cavity,
CC       resembling the structure of eukaryotic proteasomes. Component of the
CC       ClpAP and ClpXP complexes. {ECO:0000255|HAMAP-Rule:MF_00444,
CC       ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:16682229,
CC       ECO:0000269|PubMed:20637416, ECO:0000269|PubMed:20851345,
CC       ECO:0000269|PubMed:9390554}.
CC   -!- INTERACTION:
CC       P0A6G7; P0ABH9: clpA; NbExp=11; IntAct=EBI-370625, EBI-546140;
CC       P0A6G7; P0A6G7: clpP; NbExp=9; IntAct=EBI-370625, EBI-370625;
CC       P0A6G7; P0A6H1: clpX; NbExp=5; IntAct=EBI-370625, EBI-547386;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By heat shock. Part of the clpP-clpX operon.
CC       {ECO:0000269|PubMed:8093059}.
CC   -!- DOMAIN: The N-terminus (residues 17-34) interact with ClpA and ClpX.
CC       {ECO:0000269|PubMed:16406682}.
CC   -!- DISRUPTION PHENOTYPE: Cells undergo an apoptotic-like death upon DNA
CC       damage characterized by membrane depolarization (PubMed:22412352).
CC       Decreased persister cell formation upon antibiotic challenge probably
CC       due to increased levels of MazF toxin (PubMed:24375411).
CC       {ECO:0000269|PubMed:22412352, ECO:0000269|PubMed:24375411}.
CC   -!- MISCELLANEOUS: Acyldepsipeptide antibiotics bind in the ClpA or ClpX
CC       binding-sites, rendering the enzyme ATP-independent and indiscriminate,
CC       thus killing cells. {ECO:0000305|PubMed:20851345}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
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DR   EMBL; J05534; AAA23588.1; -; Genomic_DNA.
DR   EMBL; U82664; AAB40193.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73540.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76217.1; -; Genomic_DNA.
DR   PIR; B36575; B36575.
DR   RefSeq; NP_414971.1; NC_000913.3.
DR   RefSeq; WP_000122253.1; NZ_STEB01000007.1.
DR   PDB; 1TYF; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=15-207.
DR   PDB; 1YG6; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=15-207.
DR   PDB; 1YG8; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=18-207.
DR   PDB; 2FZS; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=15-207.
DR   PDB; 3HLN; X-ray; 3.20 A; 1/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=15-207.
DR   PDB; 3MT6; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-207.
DR   PDB; 6NB1; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-207.
DR   PDB; 6PO1; EM; 4.20 A; H/I/J/K/L/M/N=1-207.
DR   PDB; 6PO3; EM; 4.28 A; H/I/J/K/L/M/N=1-207.
DR   PDB; 6POD; EM; 4.05 A; H/I/J/K/L/M/N=1-207.
DR   PDB; 6POS; EM; 4.12 A; H/I/J/K/L/M/N=1-207.
DR   PDB; 6PPE; EM; 3.19 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=16-207.
DR   PDB; 6UQE; EM; 3.00 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=15-206.
DR   PDB; 6UQO; EM; 3.10 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=15-206.
DR   PDB; 6W1Z; EM; 2.70 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-207.
DR   PDB; 6W20; EM; 3.00 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-207.
DR   PDB; 6W21; EM; 3.30 A; G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-207.
DR   PDB; 6WR2; EM; 2.88 A; H/I/J/K/L/M/N/h/i/j/k/l/m/n=16-207.
DR   PDB; 6WRF; EM; 3.14 A; H/I/J/K/L/M/N=16-207.
DR   PDB; 6WSG; EM; 3.16 A; H/I/J/K/L/M/N=16-207.
DR   PDB; 7MK5; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=15-207.
DR   PDB; 7UIV; EM; 3.38 A; H/I/J/K/L/M/N=15-207.
DR   PDB; 7UIW; EM; 3.33 A; H/I/J/K/L/M/N=15-207.
DR   PDB; 7UIX; EM; 3.24 A; H/I/J/K/L/M/N=15-207.
DR   PDB; 7UIY; EM; 3.22 A; H/I/J/K/L/M/N=15-207.
DR   PDB; 7UIZ; EM; 3.24 A; H/I/J/K/L/M/N=15-207.
DR   PDB; 7UJ0; EM; 3.26 A; H/I/J/K/L/M/N=15-207.
DR   PDB; 8E7V; EM; 3.10 A; H/I/J/K/L/M/N/h/i/j/k/l/m/n=16-207.
DR   PDB; 8E8Q; EM; 3.12 A; H/I/J/K/L/M/N/h/i/j/k/l/m/n=16-207.
DR   PDB; 8E91; EM; 2.57 A; H/I/J/K/L/M/N/h/i/j/k/l/m/n=16-207.
DR   PDB; 8ET3; EM; 3.70 A; H/I/J/K/L/M/N=16-207.
DR   PDBsum; 1TYF; -.
DR   PDBsum; 1YG6; -.
DR   PDBsum; 1YG8; -.
DR   PDBsum; 2FZS; -.
DR   PDBsum; 3HLN; -.
DR   PDBsum; 3MT6; -.
DR   PDBsum; 6NB1; -.
DR   PDBsum; 6PO1; -.
DR   PDBsum; 6PO3; -.
DR   PDBsum; 6POD; -.
DR   PDBsum; 6POS; -.
DR   PDBsum; 6PPE; -.
DR   PDBsum; 6UQE; -.
DR   PDBsum; 6UQO; -.
DR   PDBsum; 6W1Z; -.
DR   PDBsum; 6W20; -.
DR   PDBsum; 6W21; -.
DR   PDBsum; 6WR2; -.
DR   PDBsum; 6WRF; -.
DR   PDBsum; 6WSG; -.
DR   PDBsum; 7MK5; -.
DR   PDBsum; 7UIV; -.
DR   PDBsum; 7UIW; -.
DR   PDBsum; 7UIX; -.
DR   PDBsum; 7UIY; -.
DR   PDBsum; 7UIZ; -.
DR   PDBsum; 7UJ0; -.
DR   PDBsum; 8E7V; -.
DR   PDBsum; 8E8Q; -.
DR   PDBsum; 8E91; -.
DR   PDBsum; 8ET3; -.
DR   AlphaFoldDB; P0A6G7; -.
DR   EMDB; EMD-20406; -.
DR   EMDB; EMD-20408; -.
DR   EMDB; EMD-20412; -.
DR   EMDB; EMD-20418; -.
DR   EMDB; EMD-20434; -.
DR   EMDB; EMD-20845; -.
DR   EMDB; EMD-20851; -.
DR   EMDB; EMD-21519; -.
DR   EMDB; EMD-21520; -.
DR   EMDB; EMD-21521; -.
DR   EMDB; EMD-21875; -.
DR   EMDB; EMD-21882; -.
DR   EMDB; EMD-21892; -.
DR   EMDB; EMD-27941; -.
DR   EMDB; EMD-27946; -.
DR   EMDB; EMD-27952; -.
DR   EMDB; EMD-28585; -.
DR   SMR; P0A6G7; -.
DR   BioGRID; 4260736; 465.
DR   BioGRID; 849471; 1.
DR   ComplexPortal; CPX-3175; Endopeptidase ClpAP complex.
DR   ComplexPortal; CPX-3176; Endopeptidase ClpXP complex.
DR   ComplexPortal; CPX-3178; Endopeptidase ClpP complex.
DR   DIP; DIP-31838N; -.
DR   IntAct; P0A6G7; 68.
DR   STRING; 511145.b0437; -.
DR   BindingDB; P0A6G7; -.
DR   ChEMBL; CHEMBL3341578; -.
DR   DrugBank; DB07571; N~2~-[(BENZYLOXY)CARBONYL]-N-[(1S,2S)-2-HYDROXY-1-(4-HYDROXYBENZYL)PROPYL]-L-LEUCINAMIDE.
DR   MEROPS; S14.001; -.
DR   jPOST; P0A6G7; -.
DR   PaxDb; 511145-b0437; -.
DR   EnsemblBacteria; AAC73540; AAC73540; b0437.
DR   GeneID; 83577599; -.
DR   GeneID; 945082; -.
DR   KEGG; ecj:JW0427; -.
DR   KEGG; eco:b0437; -.
DR   PATRIC; fig|1411691.4.peg.1839; -.
DR   EchoBASE; EB0156; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_3_2_6; -.
DR   InParanoid; P0A6G7; -.
DR   OMA; RDYWMKA; -.
DR   OrthoDB; 9802800at2; -.
DR   PhylomeDB; P0A6G7; -.
DR   BioCyc; EcoCyc:EG10158-MONOMER; -.
DR   BioCyc; MetaCyc:EG10158-MONOMER; -.
DR   BRENDA; 3.4.21.92; 2026.
DR   EvolutionaryTrace; P0A6G7; -.
DR   PRO; PR:P0A6G7; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR   GO; GO:0009368; C:endopeptidase Clp complex; IPI:ComplexPortal.
DR   GO; GO:0009376; C:HslUV protease complex; IDA:CAFA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:CAFA.
DR   GO; GO:0051117; F:ATPase binding; IPI:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; IDA:EcoCyc.
DR   GO; GO:0043068; P:positive regulation of programmed cell death; IMP:CACAO.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IMP:CACAO.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IDA:CAFA.
DR   GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR   GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR   GO; GO:0009266; P:response to temperature stimulus; EXP:EcoCyc.
DR   CDD; cd07017; S14_ClpP_2; 1.
DR   HAMAP; MF_00444; ClpP; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR023562; ClpP/TepA.
DR   InterPro; IPR033135; ClpP_His_AS.
DR   InterPro; IPR018215; ClpP_Ser_AS.
DR   NCBIfam; TIGR00493; clpP; 1.
DR   PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10381:SF70; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; 1.
DR   SWISS-2DPAGE; P0A6G7; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Protease;
KW   Reference proteome; Serine protease; Stress response; Zymogen.
FT   PROPEP          1..14
FT                   /evidence="ECO:0000269|PubMed:2197275"
FT                   /id="PRO_0000268012"
FT   CHAIN           15..207
FT                   /note="ATP-dependent Clp protease proteolytic subunit"
FT                   /id="PRO_0000179551"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         17
FT                   /note="V->A: No ClpA-ClpP, little ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         18
FT                   /note="P->A: Reduced processing, no ClpA-ClpP complex
FT                   forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         19
FT                   /note="M->A: No ClpA-ClpP, little ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         20
FT                   /note="V->A: No ClpA-ClpP or ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         21
FT                   /note="I->A: No ClpA-ClpP or ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         24
FT                   /note="T->A: No ClpA-ClpP, little ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         27
FT                   /note="G->A: No ClpA-ClpP, little ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         32
FT                   /note="D->A: No ClpA-ClpP or ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         33
FT                   /note="I->A: No ClpA-ClpP or ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         34
FT                   /note="Y->A: No ClpA-ClpP or ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         126
FT                   /note="F->A: Little ClpA-ClpP or ClpX-ClpP complex forms."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   MUTAGEN         185
FT                   /note="D->A: Loss of protease activity, forms ClpA-ClpP
FT                   complex."
FT                   /evidence="ECO:0000269|PubMed:16406682"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:2FZS"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:6NB1"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:2FZS"
FT   HELIX           33..38
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   HELIX           51..67
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          101..110
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   HELIX           112..118
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:7UIW"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          132..135
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          139..145
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   HELIX           146..171
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   HELIX           175..181
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   TURN            182..185
FT                   /evidence="ECO:0007829|PDB:3HLN"
FT   STRAND          186..189
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   HELIX           190..195
FT                   /evidence="ECO:0007829|PDB:1YG6"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:1YG6"
SQ   SEQUENCE   207 AA;  23187 MW;  A7843D036C8CB3C2 CRC64;
     MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE DHMANLIVAQ
     MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD VSTICMGQAA SMGAFLLTAG
     AKGKRFCLPN SRVMIHQPLG GYQGQATDIE IHAREILKVK GRMNELMALH TGQSLEQIER
     DTERDRFLSA PEAVEYGLVD SILTHRN
//