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ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Caseinolytic protease) (Endopeptidase Clp) (Heat shock protein F21.5) (Protease Ti)

 CLPP_ECOLI              Reviewed;         207 AA.
P0A6G7; P19245; Q2MBY9;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 1.
28-MAR-2018, entry version 122.
RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
AltName: Full=Caseinolytic protease;
AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
AltName: Full=Heat shock protein F21.5;
AltName: Full=Protease Ti;
Flags: Precursor;
Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=lopP;
OrderedLocusNames=b0437, JW0427;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 15-36.
PubMed=2197275;
Maurizi M.R., Clark W.P., 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. 265:12536-12545(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
IDENTIFICATION AS A HEAT SHOCK PROTEIN.
PubMed=2211522; DOI=10.1128/jb.172.10.6026-6034.1990;
Kroh H.E., Simon L.D.;
"The ClpP component of Clp protease is the sigma 32-dependent heat
shock protein F21.5.";
J. Bacteriol. 172:6026-6034(1990).
[6]
CHARACTERIZATION.
PubMed=8407953;
Arribas J., Castano J.G.;
"A comparative study of the chymotrypsin-like activity of the rat
liver multicatalytic proteinase and the ClpP from Escherichia coli.";
J. Biol. Chem. 268:21165-21171(1993).
[7]
INDUCTION, AND OPERON.
PubMed=8093059; DOI=10.1006/bbrc.1994.2253;
Yoo S.J., Seol J.H., Kang M.S., Ha D.B., Chung C.H.;
"clpX encoding an alternative ATP-binding subunit of protease Ti (Clp)
can be expressed independently from clpP in Escherichia coli.";
Biochem. Biophys. Res. Commun. 203:798-804(1994).
[8]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[9]
FUNCTION.
PubMed=12941278; DOI=10.1016/S0092-8674(03)00612-3;
Kenniston J.A., Baker T.A., Fernandez J.M., Sauer R.T.;
"Linkage between ATP consumption and mechanical unfolding during the
protein processing reactions of an AAA+ degradation machine.";
Cell 114:511-520(2003).
[10]
FUNCTION, AND SUBSTRATE.
PubMed=15371343; DOI=10.1101/gad.1240104;
Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
"Modulating substrate choice: the SspB adaptor delivers a regulator of
the extracytoplasmic-stress response to the AAA+ protease ClpXP for
degradation.";
Genes Dev. 18:2292-2301(2004).
[11]
DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=22412352; DOI=10.1371/journal.pbio.1001281;
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. 10:E1001281-E1001281(2012).
[12]
CLEAVAGE OF ANTITOXIN MAZE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / BW25113, and K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=24375411; DOI=10.1074/jbc.M113.510511;
Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.;
"MazF-induced growth inhibition and persister generation in
Escherichia coli.";
J. Biol. Chem. 289:4191-4205(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8831780; DOI=10.1006/jmbi.1996.0499;
Shin D.H., Lee C.S., Chung C.H., Suh S.W.;
"Molecular symmetry of the ClpP component of the ATP-dependent Clp
protease, an Escherichia coli homolog of 20 S proteasome.";
J. Mol. Biol. 262:71-76(1996).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 15-207, AND SUBUNIT.
PubMed=9390554; DOI=10.1016/S0092-8674(00)80431-6;
Wang J., Hartling J.A., Flanagan J.M.;
"The structure of ClpP at 2.3-A resolution suggests a model for ATP-
dependent proteolysis.";
Cell 91:447-456(1997).
[15]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, DOMAIN, AND MUTAGENESIS OF VAL-17; PRO-18;
MET-19; VAL-20; ILE-21; THR-24; GLY-27; ASP-32; ILE-33; TYR-34;
PHE-126 AND ASP-185.
PubMed=16406682; DOI=10.1016/j.jsb.2005.09.011;
Bewley M.C., Graziano V., Griffin K., Flanagan J.M.;
"The asymmetry in the mature amino-terminus of ClpP facilitates a
local symmetry match in ClpAP and ClpXP complexes.";
J. Struct. Biol. 153:113-128(2006).
[16]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 15-207 BOUND TO INHIBITOR,
ENZYME REGULATION, AND SUBUNIT.
PubMed=16682229; DOI=10.1016/j.jsb.2006.03.013;
Szyk A., Maurizi M.R.;
"Crystal structure at 1.9 A of E. coli ClpP with a peptide covalently
bound at the active site.";
J. Struct. Biol. 156:165-174(2006).
[17]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ANTIBIOTIC, AND
SUBUNIT.
PubMed=20851345; DOI=10.1016/j.chembiol.2010.07.008;
Li D.H., Chung Y.S., Gloyd M., Joseph E., Ghirlando R., Wright G.D.,
Cheng Y.Q., Maurizi M.R., 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. 17:959-969(2010).
[18]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 15-207, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
PubMed=20637416; DOI=10.1016/j.str.2010.04.008;
Kimber M.S., Yu A.Y., Borg M., Leung E., Chan H.S., Houry W.A.;
"Structural and theoretical studies indicate that the cylindrical
protease ClpP samples extended and compact conformations.";
Structure 18:798-808(2010).
-!- 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). {ECO:0000255|HAMAP-
Rule:MF_00444, ECO:0000269|PubMed:12941278,
ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:24375411}.
-!- CATALYTIC ACTIVITY: 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). {ECO:0000255|HAMAP-
Rule:MF_00444}.
-!- ENZYME REGULATION: Inhibited by benzyloxycarbonyl leucyltyrosine
chloromethylketone (Z-LY-CMK). {ECO:0000269|PubMed:16682229}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin (N-
succinyl-Leu-Tyr-AMC) {ECO:0000269|PubMed:16406682,
ECO:0000269|PubMed:20637416};
KM=1.0 mM for N-succinyl-Leu-Tyr-AMC
{ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:20637416};
-!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
which stack back to back to give a disk-like structure with a
central cavity, resembling the structure of eukaryotic
proteasomes. Component of the ClpAP and ClpXP complexes.
{ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:16406682,
ECO:0000269|PubMed:16682229, ECO:0000269|PubMed:20637416,
ECO:0000269|PubMed:20851345, ECO:0000269|PubMed:9390554}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-370625, EBI-370625;
P0ABH9:clpA; NbExp=11; IntAct=EBI-370625, EBI-546140;
P0A6H1:clpX; NbExp=5; IntAct=EBI-370625, EBI-547386;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: By heat shock. Part of the clpP-clpX operon.
{ECO:0000269|PubMed:8093059}.
-!- DOMAIN: The N-terminus (residues 17-34) interact with ClpA and
ClpX. {ECO:0000269|PubMed:16406682}.
-!- DISRUPTION PHENOTYPE: Cells undergo an apoptotic-like death upon
DNA damage characterized by membrane depolarization
(PubMed:22412352). Decreased persister cell formation upon
antibotic challenge probably due to increased levels of MazF toxin
(PubMed:24375411). {ECO:0000269|PubMed:22412352,
ECO:0000269|PubMed:24375411}.
-!- MISCELLANEOUS: Acyldepsipeptide antibiotics bind in the ClpA or
ClpX binding-sites, rendering the enzyme ATP-independent and
indiscriminate, thus killing cells. {ECO:0000305|PubMed:20851345}.
-!- SIMILARITY: Belongs to the peptidase S14 family.
{ECO:0000255|HAMAP-Rule:MF_00444}.
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EMBL; J05534; AAA23588.1; -; Genomic_DNA.
EMBL; U82664; AAB40193.1; -; Genomic_DNA.
EMBL; U00096; AAC73540.1; -; Genomic_DNA.
EMBL; AP009048; BAE76217.1; -; Genomic_DNA.
PIR; B36575; B36575.
RefSeq; NP_414971.1; NC_000913.3.
RefSeq; WP_000122253.1; NZ_LN832404.1.
PDB; 1TYF; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=15-207.
PDB; 1YG6; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=15-207.
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.
PDB; 2FZS; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=15-207.
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.
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.
PDBsum; 1TYF; -.
PDBsum; 1YG6; -.
PDBsum; 1YG8; -.
PDBsum; 2FZS; -.
PDBsum; 3HLN; -.
PDBsum; 3MT6; -.
ProteinModelPortal; P0A6G7; -.
SMR; P0A6G7; -.
BioGrid; 4260736; 465.
DIP; DIP-31838N; -.
IntAct; P0A6G7; 68.
STRING; 316385.ECDH10B_0393; -.
BindingDB; P0A6G7; -.
ChEMBL; CHEMBL3341578; -.
SWISS-2DPAGE; P0A6G7; -.
EPD; P0A6G7; -.
PaxDb; P0A6G7; -.
PRIDE; P0A6G7; -.
EnsemblBacteria; AAC73540; AAC73540; b0437.
EnsemblBacteria; BAE76217; BAE76217; BAE76217.
GeneID; 945082; -.
KEGG; ecj:JW0427; -.
KEGG; eco:b0437; -.
PATRIC; fig|1411691.4.peg.1839; -.
EchoBASE; EB0156; -.
EcoGene; EG10158; clpP.
eggNOG; ENOG4105CCQ; Bacteria.
eggNOG; COG0740; LUCA.
HOGENOM; HOG000285833; -.
InParanoid; P0A6G7; -.
KO; K01358; -.
OMA; LFLQSEN; -.
PhylomeDB; P0A6G7; -.
BioCyc; EcoCyc:EG10158-MONOMER; -.
BioCyc; MetaCyc:EG10158-MONOMER; -.
EvolutionaryTrace; P0A6G7; -.
PRO; PR:P0A6G7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0009376; C:HslUV protease complex; IDA:CAFA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:CAFA.
GO; GO:0051117; F:ATPase binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:EcoCyc.
GO; GO:0010498; P:proteasomal protein catabolic process; IMP:CACAO.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:MGI.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
GO; GO:0009266; P:response to temperature stimulus; EXP:EcoCyc.
CDD; cd07017; S14_ClpP_2; 1.
HAMAP; MF_00444; ClpP; 1.
InterPro; IPR001907; ClpP.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR023562; ClpP/TepA.
InterPro; IPR033135; ClpP_His_AS.
InterPro; IPR018215; ClpP_Ser_AS.
PANTHER; PTHR10381; PTHR10381; 1.
Pfam; PF00574; CLP_protease; 1.
PRINTS; PR00127; CLPPROTEASEP.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR00493; clpP; 1.
PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PROSITE; PS00381; CLP_PROTEASE_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Protease; Reference proteome; Serine protease;
Stress response; Zymogen.
PROPEP 1 14 {ECO:0000269|PubMed:2197275}.
/FTId=PRO_0000268012.
CHAIN 15 207 ATP-dependent Clp protease proteolytic
subunit.
/FTId=PRO_0000179551.
ACT_SITE 111 111 Nucleophile. {ECO:0000305}.
ACT_SITE 136 136 {ECO:0000305}.
ACT_SITE 185 185 {ECO:0000305}.
MUTAGEN 17 17 V->A: No ClpA-ClpP, little ClpX-ClpP
complex forms.
{ECO:0000269|PubMed:16406682}.
MUTAGEN 18 18 P->A: Reduced processing, no ClpA-ClpP
complex forms.
{ECO:0000269|PubMed:16406682}.
MUTAGEN 19 19 M->A: No ClpA-ClpP, little ClpX-ClpP
complex forms.
{ECO:0000269|PubMed:16406682}.
MUTAGEN 20 20 V->A: No ClpA-ClpP or ClpX-ClpP complex
forms. {ECO:0000269|PubMed:16406682}.
MUTAGEN 21 21 I->A: No ClpA-ClpP or ClpX-ClpP complex
forms. {ECO:0000269|PubMed:16406682}.
MUTAGEN 24 24 T->A: No ClpA-ClpP, little ClpX-ClpP
complex forms.
{ECO:0000269|PubMed:16406682}.
MUTAGEN 27 27 G->A: No ClpA-ClpP, little ClpX-ClpP
complex forms.
{ECO:0000269|PubMed:16406682}.
MUTAGEN 32 32 D->A: No ClpA-ClpP or ClpX-ClpP complex
forms. {ECO:0000269|PubMed:16406682}.
MUTAGEN 33 33 I->A: No ClpA-ClpP or ClpX-ClpP complex
forms. {ECO:0000269|PubMed:16406682}.
MUTAGEN 34 34 Y->A: No ClpA-ClpP or ClpX-ClpP complex
forms. {ECO:0000269|PubMed:16406682}.
MUTAGEN 126 126 F->A: Little ClpA-ClpP or ClpX-ClpP
complex forms.
{ECO:0000269|PubMed:16406682}.
MUTAGEN 185 185 D->A: Loss of protease activity, forms
ClpA-ClpP complex.
{ECO:0000269|PubMed:16406682}.
STRAND 19 21 {ECO:0000244|PDB:2FZS}.
STRAND 22 24 {ECO:0000244|PDB:1YG6}.
STRAND 27 29 {ECO:0000244|PDB:3MT6}.
STRAND 30 32 {ECO:0000244|PDB:2FZS}.
HELIX 33 38 {ECO:0000244|PDB:1YG6}.
TURN 39 41 {ECO:0000244|PDB:1YG6}.
STRAND 42 49 {ECO:0000244|PDB:1YG6}.
HELIX 51 67 {ECO:0000244|PDB:1YG6}.
STRAND 69 71 {ECO:0000244|PDB:1YG6}.
STRAND 73 79 {ECO:0000244|PDB:1YG6}.
HELIX 84 96 {ECO:0000244|PDB:1YG6}.
STRAND 97 99 {ECO:0000244|PDB:1YG6}.
STRAND 101 110 {ECO:0000244|PDB:1YG6}.
HELIX 112 118 {ECO:0000244|PDB:1YG6}.
STRAND 125 127 {ECO:0000244|PDB:1YG6}.
STRAND 132 135 {ECO:0000244|PDB:1YG6}.
STRAND 139 145 {ECO:0000244|PDB:1YG6}.
HELIX 146 171 {ECO:0000244|PDB:1YG6}.
HELIX 175 181 {ECO:0000244|PDB:1YG6}.
TURN 182 185 {ECO:0000244|PDB:3HLN}.
STRAND 186 189 {ECO:0000244|PDB:1YG6}.
HELIX 190 195 {ECO:0000244|PDB:1YG6}.
STRAND 198 202 {ECO:0000244|PDB:1YG6}.
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


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E0800h ELISA Homo sapiens,Human,IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,PAPPA,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
E0800m ELISA kit IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protei 96T


 

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