Reviewed, UniProtKB/Swiss-Prot Q9S834 (CLPP5_ARATH)

Names and origin

Protein names

Recommended name:
    ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase ClpP5
      Short name=nClpP5
    nClpP1

Gene names

Name:	CLPP5
Synonyms:	NCLPP1, NCLPP5
Ordered Locus Names:	At1g02560
ORF Names:	T14P4.12

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	298 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).
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.
Subcellular location	Plastid › chloroplast stroma.
Tissue specificity	Mostly expressed in leaves. Also detected in stems, and to a lower extent, in roots (at protein level).
Induction	Repressed in darkness. Induced by high light stress and during cold acclimation (at protein level).
Sequence similarities	Belongs to the peptidase S14 family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR plastid stroma Ref.8 Inferred from direct assay. Source: TAIR stromule Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR
Molecular function	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
	Transit peptide	1 – 62	62	Chloroplast Potential
	Chain	63 – 298	236	ATP-dependent Clp protease proteolytic subunit 5, chloroplastic		PRO_0000308980
Sites
	Active site	193	1	By similarity
	Active site	218	1	By similarity
Experimental info
	Sequence conflict	115	1	I → II AA sequence Ref.6
	Sequence conflict	246	1	N → D AA sequence Ref.6
	Sequence conflict	253	1	Missing AA sequence Ref.6
	Sequence conflict	267	1	Missing AA sequence Ref.6
	Sequence conflict	280	1	L → I AA sequence Ref.6
	Sequence conflict	285	1	I → L AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9S834-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 0B550019A2F6A33C	FASTA	298	32,356
	10 20 30 40 50 60 MAHACVSTSA SSLRFTAGFV SASPNGSSFD SPKLSLPFEP LRSRKTNKLV SDRKNWKNST 70 80 90 100 110 120 PKAVYSGNLW TPEIPSPQGV WSIRDDLQVP SSPYFPAYAQ GQGPPPMVQE RFQSIISQLF 130 140 150 160 170 180 QYRIIRCGGA VDDDMANIIV AQLLYLDAVD PTKDIVMYVN SPGGSVTAGM AIFDTMRHIR 190 200 210 220 230 240 PDVSTVCVGL AASMGAFLLS AGTKGKRYSL PNSRIMIHQP LGGAQGGQTD IDIQANEMLH 250 260 270 280 290 HKANLNGYLA YHTGQSLEKI NQDTDRDFFM SAKEAKEYGL IDGVIMNPLK ALQPLAAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 [MRNA], INDUCTION. Strain: cv. Columbia.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION. Strain: cv. Columbia. Tissue: Hypocotyl.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Kim C.J., Chen H., Shinn P., Ecker J.R. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"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 112-123; 243-273 AND 277-290, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[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.
[8]	"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: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION.
[9]	"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.
[10]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB022326 mRNA. Translation: BAA82065.1.
AJ012278 mRNA. Translation: CAB43488.1.
AC022521 Genomic DNA. Translation: AAG10637.1.
BT024859 mRNA. Translation: ABD65590.1.
AY084394 mRNA. Translation: AAM60971.1.

PIR

T52455.

RefSeq

NP_563657.1.

UniGene

At.21093

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R92	model	-	A	1-298	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S14.001.

Proteomic databases

ProMEX

Q9S834.

Genome annotation databases

GeneID

839433.

GenomeReviews

Gene locus AT1G02560 in contig CT485782_GR.

KEGG

ath:AT1G02560.

NMPDR

fig|3702.1.peg.377.

Organism-specific databases

GeneFarm

806. 98.

TAIR

At1g02560.

Family and domain databases

InterPro

IPR001907. Pept_S14_ClpP.
[Graphical view]

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

CLPP5_ARATH

Accession

Primary (citable) accession number: Q9S834

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 2000
Last modified:	November 25, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)