ATP-dependent Clp protease proteolytic subunit 2, mitochondrial precursor

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Q9FN42 (CLPP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 69. 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 2, mitochondrial
EC=3.4.21.92

Alternative name(s):
Endopeptidase ClpP2
nClpP7

Gene names

Name:	CLPP2
Synonyms:	NCLPP7
Ordered Locus Names:	At5g23140
ORF Names:	MYJ24.13

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	241 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 By similarity.
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).
Subcellular location	Mitochondrion Ref.6.
Tissue specificity	Constitutively expressed in leaves, shoots, roots and flowers. Ref.6
Sequence similarities	Belongs to the peptidase S14 family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast thylakoid membrane Inferred from direct assay Ref.5. Source: TAIR chloroplastic endopeptidase Clp complex Inferred from direct assay Ref.5. Source: TAIR mitochondrion Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from direct assay. Source: TAIR serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

Mitochondrion Potential

Chain

31 – 241

211

ATP-dependent Clp protease proteolytic subunit 2, mitochondrial

PRO_0000308977

Sites

Active site

127

By similarity

Active site

152

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FN42 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: DFC93372387E542A
Show »

FASTA

241

26,283

        10         20         30         40         50         60 
MMRGLVSGAK MLSSTPSSMA TSIATGRRSY SLIPMVIEHS SRGERAYDIF SRLLKERIIC 

        70         80         90        100        110        120 
INGPINDDTS HVVVAQLLYL ESENPSKPIH MYLNSPGGHV TAGLAIYDTM QYIRSPISTI 

       130        140        150        160        170        180 
CLGQAASMAS LLLAAGAKGQ RRSLPNATVM IHQPSGGYSG QAKDITIHTK QIVRVWDALN 

       190        200        210        220        230        240 
ELYVKHTGQP LDVVANNMDR DHFMTPEEAK AFGIIDEVID ERPLELVKDA VGNESKDKSS 


S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones." Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:291-300(1997) [PubMed: 9405937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana." Peltier J.-B., Ytterberg J., Liberles D.A., Roepstorff P., van Wijk K.J. J. Biol. Chem. 276:16318-16327(2001) [PubMed: 11278690] [Abstract] Cited for: PROTEIN SEQUENCE OF 143-163; 175-185 AND 211-228, IDENTIFICATION BY MASS SPECTROMETRY.
[6]	"Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease." Halperin T., Zheng B., Itzhaki H., Clarke A.K., Adam Z. Plant Mol. Biol. 45:461-468(2001) [PubMed: 11352464] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature." Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K., Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K. Plant Physiol. 125:1912-1918(2001) [PubMed: 11299370] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB006708 Genomic DNA. Translation: BAB09831.1.
CP002688 Genomic DNA. Translation: AED93126.1.
AK118523 mRNA. Translation: BAC43126.1.
BT005261 mRNA. Translation: AAO63325.1.

IPI

IPI00533430.

RefSeq

NP_568427.1. NM_122220.4.

UniGene

At.31024.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R8V	model	-	A	1-241	[»]

ProteinModelPortal

Q9FN42.

SMR

Q9FN42. Positions 31-223.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9FN42.

Protein family/group databases

MEROPS

S14.A02.

Proteomic databases

PRIDE

Q9FN42.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G23140.1; AT5G23140.1; AT5G23140.

GeneID

832378.

GenomeReviews

Gene locus AT5G23140 in contig BA000015_GR.

KEGG

ath:AT5G23140.

NMPDR

fig|3702.1.peg.24485.

Organism-specific databases

GeneFarm

805. 98.

TAIR

At5g23140.

Phylogenomic databases

eggNOG

KOG0840.

GeneTree

EPGT00070000029122.

HOGENOM

HBG558421.

InParanoid

Q9FN42.

OMA

NELYVKH.

PhylomeDB

Q9FN42.

ProtClustDB

CLSN2917700.

Gene expression databases

Genevestigator

Q9FN42.

Family and domain databases

InterPro

IPR023562. Pept_S14/S49.
IPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]

K01358.

PANTHER

PTHR10381. Pept_S14_ClpP. 1 hit.

Pfam

PF00574. CLP_protease. 1 hit.
[Graphical view]

PRINTS

PR00127. CLPPROTEASEP.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

CLPP2_ARATH

Accession

Primary (citable) accession number: Q9FN42

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	March 1, 2001
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents