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Reviewed, UniProtKB/Swiss-Prot Q36863 (CLPP1_CYAPA)

Last modified January 19, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP-dependent Clp protease proteolytic subunit
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp
Gene names
Name: clpP-A
Synonyms: clpP1
Encoded onPlastid; Cyanelle
OrganismCyanophora paradoxa
Taxonomic identifier2762 [NCBI]
Taxonomic lineageEukaryotaGlaucocystophyceaeCyanophoraceaeCyanophora

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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. HAMAP MF_00444

Subcellular location

Plastidcyanelle HAMAP MF_00444.

Sequence similarities

Belongs to the peptidase S14 family.

Ontologies

Keywords
   Cellular componentCyanelle
Plastid
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcyanelle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194ATP-dependent Clp protease proteolytic subunit HAMAP MF_00444
PRO_0000179728

Sites

Active site981 By similarity
Active site1231 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q36863-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7F519941355BF3A2

FASTA19421,816
        10         20         30         40         50         60 
MTILIQQYTN DENKKLELNN ISKLLQNRII LFSQTVDDEI CNSIVGQLLY LENEDSTKDI 

        70         80         90        100        110        120 
RLFINSPGGS VTAGLSVYDT IQNLSVDVST ICFGLAASMG AVLLAAGVEN KRFAFASSRI 

       130        140        150        160        170        180 
MIHQPLSKVE APWSHLDIQI RNGAYFKNLL NNILSFHTKQ ELKQIETDTE RDFFLSATEA 

       190 
KQYGIIDHIF INNN 

« Hide

References

[1]"Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."
Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., Bryant D.A.
Plant Mol. Biol. Rep. 13:327-332(1995)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTEX LB 555 / Pringsheim.
[2]"The complete sequence of the cyanelle genome of Cyanophora paradoxa: the genetic complexity of a primitive plastid."
Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A.
(In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W. (eds.); Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTEX LB 555 / Pringsheim.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30821 Genomic DNA. Translation: AAA81174.1.
U30821 Genomic DNA. Translation: AAA81292.1.
PIRT06831.
RefSeqNP_043143.1.
NP_043261.1.

3D structure databases

SMRQ36863. Positions 21-191.
ModBaseSearch...

Genome annotation databases

GeneID801572.
801684.

Enzyme and pathway databases

BRENDA3.4.21.92. 11.

Family and domain databases

HAMAPMF_00444. ClpP.
[Tree]
InterProIPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
PANTHERPTHR10381. Pept_S14_ClpP. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_CYAPA
AccessionPrimary (citable) accession number: Q36863
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents