ATP-dependent Clp protease proteolytic subunit 1 - Arabidopsis thaliana (Mouse-ear cress)

Contribute

Send feedback

Read comments (?) or add your own

P56772 (CLPP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. History...

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

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

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 1
EC=3.4.21.92

Alternative name(s):
Endopeptidase ClpP1
Short name=pClpP

Gene names

Name:	clpP1
Synonyms:	ClpP
Ordered Locus Names:	AtCg00670

Encoded on

Plastid; Chloroplast

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	196 AA.
Sequence status	Complete.
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. HAMAP 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 MF_00444
Subunit structure	Component of the chloroplastic Clp protease core complex which consist of at least 16 proteins: ClpP4 (3 copies), ClpP5 (3 copies), ClpR4 (2 copies), ClpP1 (1 copy), ClpP6 (1 copy), ClpR2 (1 copy), ClpS1 (1 copy), ClpS2 (1 copy) and 3 copies of ClpP3 and/or ClpR1 and/or ClpR3. Ref.3 Ref.7 Ref.8 Ref.9
Subcellular location	Plastid › chloroplast stroma Ref.2 Ref.6 Ref.9.
Tissue specificity	Mostly expressed in leaves. Also detected in stems, and to a lower extent, in roots (at protein level). Ref.6
Induction	Repressed in darkness. Slightly induced by high light stress and during cold acclimation (at protein level). Ref.2 Ref.6
Sequence similarities	Belongs to the peptidase S14 family.
RNA editing	Edited at position 187. Ref.4

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Coding sequence diversity	RNA editing
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 stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444

PRO_0000179734

Sites

Active site

101

By similarity

Active site

126

By similarity

Secondary structure

196

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P56772 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 2BB430CFB5B5F609
Show »

FASTA

196

22,124

        10         20         30         40         50         60 
MPIGVPKVPF RSPGEGDTSW VDIYNRLYRE RLFFLGQEVD TEISNQLISL MIYLSIEKDT 

        70         80         90        100        110        120 
KDLYLFINSP GGWVISGMAI YDTMQFVRPD VQTICMGLAA SIASFILVGG AITKRIAFPH 

       130        140        150        160        170        180 
ARVMIHQPAS SFYEAQTGEF ILEAEELLKL RETITRVYVQ RTGKPIWVIS EDMERDVFMS 

       190 
ATEAQAYGIV DLVAVQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete structure of the chloroplast genome of Arabidopsis thaliana." Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S. DNA Res. 6:283-290(1999) [PubMed: 10574454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Identification of clp genes expressed in senescing Arabidopsis leaves." Nakabayashi K., Ito M., Kiyosue T., Shinozaki K., Watanabe A. Plant Cell Physiol. 40:504-514(1999) [PubMed: 10427773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION. Strain: cv. Columbia.
[3]	"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 12-26 AND 123-149, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[4]	"Editing of plastid RNA in Arabidopsis thaliana ecotypes." Tillich M., Funk H.T., Schmitz-Linneweber C., Poltnigg P., Sabater B., Martin M., Maier R.M. Plant J. 43:708-715(2005) [PubMed: 16115067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-195, RNA EDITING. Strain: cv. Cvi-0 and cv. Wassilewskija.
[5]	"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.
[6]	"Characterization of chloroplast Clp proteins in Arabidopsis: localization, tissue specificity and stress responses." Zheng B., Halperin T., Hruskova-Heidingsfeldova O., Adam Z., Clarke A.K. Physiol. Plantarum 114:92-101(2002) [PubMed: 11982939] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Seedling.
[7]	"Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis." Rudella A., Friso G., Alonso J.M., Ecker J.R., van Wijk K.J. Plant Cell 18:1704-1721(2006) [PubMed: 16766689] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
[8]	"Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis." Sjoegren L.L.E., Stanne T.M., Zheng B., Sutinen S., Clarke A.K. Plant Cell 18:2635-2649(2006) [PubMed: 16980539] [Abstract] Cited for: SUBUNIT.
[9]	"Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications." Peltier J.-B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J., Giacomelli L., Pillardy J., van Wijk K.J. J. Biol. Chem. 279:4768-4781(2004) [PubMed: 14593120] [Abstract] Cited for: 3D-STRUCTURE MODELING, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP000423 Genomic DNA. Translation: BAA84410.1. Sequence problems.
AB022325 Genomic DNA. Translation: BAA82063.1. Sequence problems.
AJ971664 Genomic DNA. Translation: CAI99002.1. Sequence problems.
AJ971665 Genomic DNA. Translation: CAI99003.1. Sequence problems.

IPI

IPI00524325.

RefSeq

NP_051083.1. NC_000932.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R8Z	model	-	A	1-196	[»]

ProteinModelPortal

P56772.

SMR

P56772. Positions 19-195.

ModBase

Search...

Protein-protein interaction databases

IntAct

P56772. 1 interaction.

STRING

P56772.

Protein family/group databases

MEROPS

S14.002.

Proteomic databases

PRIDE

P56772.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

844734.

GenomeReviews

Gene locus ATCG00670 in contig AP000423_GR.

KEGG

ath:ArthCp048.

Organism-specific databases

TAIR

AtCg00670.

Phylogenomic databases

eggNOG

KOG0840.

GeneTree

EPGT00070000029103.

HOGENOM

HBG558421.

ProtClustDB

CHL00028.

Enzyme and pathway databases

BRENDA

3.4.21.92. 399.

Gene expression databases

Genevestigator

P56772.

GermOnline

ATCG00670. Arabidopsis thaliana.

Family and domain databases

HAMAP

MF_00444. ClpP.
[Tree]

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. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CLPP1_ARATH

Accession

Primary (citable) accession number: P56772
Secondary accession number(s): Q3ZVD5, Q9XQZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 13, 2007
Last modified:	November 16, 2011
This is version 81 of the entry and version 2 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

Secondary structure

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents