ATP-dependent Clp protease proteolytic subunit precursor

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P0A6G7 (CLPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP-dependent Clp protease proteolytic subunit
EC=3.4.21.92

Alternative name(s):
Caseinolytic protease
Endopeptidase Clp
Heat shock protein F21.5
Protease Ti

Gene names

Name:	clpP
Synonyms:	lopP
Ordered Locus Names:	b0437, JW0427

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. HAMAP-Rule MF_00444
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). HAMAP-Rule MF_00444
Subunit structure	Component of the ClpAP and ClpXP complexes. Fourteen ClpP subunits assemble into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes, and in the presence of ATP, binds to ClpA or ClpX subunits (six subunits arranged in a hexameric ring).
Subcellular location	Cytoplasm HAMAP-Rule MF_00444.
Induction	By heat shock. HAMAP-Rule MF_00444
Sequence similarities	Belongs to the peptidase S14 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	misfolded or incompletely synthesized protein catabolic process Inferred from direct assay PubMed 10754102. Source: MGI response to heat Inferred from expression pattern PubMed 8349564. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP serine-type peptidase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 14

HAMAP-Rule MF_00444

PRO_0000268012

Chain

15 – 207

193

ATP-dependent Clp protease proteolytic subunit HAMAP-Rule MF_00444

PRO_0000179551

Sites

Active site

111

Probable

Active site

136

Probable

Secondary structure

207

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6G7 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: A7843D036C8CB3C2
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FASTA

207

23,187

        10         20         30         40         50         60 
MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE DHMANLIVAQ 

        70         80         90        100        110        120 
MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD VSTICMGQAA SMGAFLLTAG 

       130        140        150        160        170        180 
AKGKRFCLPN SRVMIHQPLG GYQGQATDIE IHAREILKVK GRMNELMALH TGQSLEQIER 

       190        200 
DTERDRFLSA PEAVEYGLVD SILTHRN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli." Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S. J. Biol. Chem. 265:12536-12545(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-36.
[2]	"Sequence of minutes 4-25 of Escherichia coli." 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. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5." Kroh H.E., Simon L.D. J. Bacteriol. 172:6026-6034(1990) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A HEAT SHOCK PROTEIN.
[6]	"A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli." Arribas J., Castano J.G. J. Biol. Chem. 268:21165-21171(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[8]	"Molecular symmetry of the ClpP component of the ATP-dependent Clp protease, an Escherichia coli homolog of 20 S proteasome." Shin D.H., Lee C.S., Chung C.H., Suh S.W. J. Mol. Biol. 262:71-76(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[9]	"The structure of ClpP at 2.3-A resolution suggests a model for ATP-dependent proteolysis." Wang J., Hartling J.A., Flanagan J.M. Cell 91:447-456(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-207.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05534 Genomic DNA. Translation: AAA23588.1.
U82664 Genomic DNA. Translation: AAB40193.1.
U00096 Genomic DNA. Translation: AAC73540.1.
AP009048 Genomic DNA. Translation: BAE76217.1.

PIR

B36575.

RefSeq

NP_414971.1. NC_000913.2.
YP_488729.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TYF	X-ray	2.30	A/B/C/D/E/F/G/H/I/J/K/L/M/N	15-207	[»]
1YG6	X-ray	1.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N	15-207	[»]
1YG8	X-ray	2.60	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	[»]
2FZS	X-ray	1.90	A/B/C/D/E/F/G/H/I/J/K/L/M/N	15-207	[»]
3HLN	X-ray	3.20	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	[»]
3MT6	X-ray	1.90	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	[»]

ProteinModelPortal

P0A6G7.

SMR

P0A6G7. Positions 16-207.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31838N.

IntAct

P0A6G7. 66 interactions.

STRING

511145.b0437.

2D gel databases

SWISS-2DPAGE

P0A6G7.

Proteomic databases

PaxDb

P0A6G7.

PRIDE

P0A6G7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73540; AAC73540; b0437.
BAE76217; BAE76217; BAE76217.

GeneID

12931742.
945082.

KEGG

ecj:Y75_p0425.
eco:b0437.

PATRIC

32116027. VBIEscCol129921_0455.

Organism-specific databases

EchoBASE

EB0156.

EcoGene

EG10158. clpP.

Phylogenomic databases

eggNOG

COG0740.

HOGENOM

HOG000285833.

K01358.

OMA

LVHPPQA.

ProtClustDB

PRK00277.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10158-MONOMER.
ECOL316407:JW0427-MONOMER.
MetaCyc:EG10158-MONOMER.

Gene expression databases

Genevestigator

P0A6G7.

Family and domain databases

HAMAP

MF_00444. ClpP.

InterPro

IPR001907. ClpP.
IPR023562. ClpP/TepA.
IPR018215. ClpP_AS.
[Graphical view]

PANTHER

PTHR10381. PTHR10381. 1 hit.

Pfam

PF00574. CLP_protease. 1 hit.
[Graphical view]

PRINTS

PR00127. CLPPROTEASEP.

TIGRFAMs

TIGR00493. clpP. 1 hit.

PROSITE

PS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6G7.

Entry information

Entry name

CLPP_ECOLI

Accession

Primary (citable) accession number: P0A6G7
Secondary accession number(s): P19245, Q2MBY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents