CLPP_ECOLI
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 03-AUG-2022, entry version 149.
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; Proteobacteria; 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 (N-
CC succinyl-Leu-Tyr-AMC) {ECO:0000269|PubMed:16406682,
CC ECO:0000269|PubMed:20637416};
CC KM=1.0 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 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 AlphaFoldDB; P0A6G7; -.
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 SWISS-2DPAGE; P0A6G7; -.
DR jPOST; P0A6G7; -.
DR PaxDb; P0A6G7; -.
DR PRIDE; P0A6G7; -.
DR EnsemblBacteria; AAC73540; AAC73540; b0437.
DR EnsemblBacteria; BAE76217; BAE76217; BAE76217.
DR GeneID; 67416488; -.
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 PhylomeDB; P0A6G7; -.
DR BioCyc; EcoCyc:EG10158-MON; -.
DR BioCyc; MetaCyc:EG10158-MON; -.
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 PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00493; clpP; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
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 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
