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Q82CA6 (CLPP3_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit 3

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp 3
Gene names
Name:clpP3
Ordered Locus Names:SAV_5447
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length219 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

Subcellular location

Cytoplasm By similarity HAMAP MF_00444.

Sequence similarities

Belongs to the peptidase S14 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 219219ATP-dependent Clp protease proteolytic subunit 3 HAMAP MF_00444
PRO_0000179661

Sites

Active site1121 By similarity
Active site1371 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82CA6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0AA2BFF372889AE5

FASTA21923,205
        10         20         30         40         50         60 
MRRPGAVVRR AGGYVTNLMP TAAGDPIGGG LGDQVYNRLL GERIIFLGQA VDDDIANKIT 

        70         80         90        100        110        120 
AQLLLLASDP DKDIYLYINS PGGSITAGMA IYDTMQYIKN DVVTIAMGMA ASMGQFLLSA 

       130        140        150        160        170        180 
GTPGKRFALP NAEILIHQPS AGLAGSASDI KIHAERLLHT KKRMAELTAF HTGQTVEQVT 

       190        200        210 
RDSDRDRWFD PVEAKEYGLI DDIMPTAAGM PGGGGTGAA 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC73159.1.
RefSeqNP_826624.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82CA6.
SMRQ82CA6. Positions 35-204.
ModBaseSearch...

Protein family/group databases

MEROPSS14.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1211276.
GenomeReviewsGene locus SAV_5447 in contig BA000030_GR.
KEGGsma:SAV_5447.
NMPDRfig|227882.1.peg.5450.
PATRIC23724880. VBIStrAve112782_5799.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG558421.
OMACDIATYG.
ProtClustDBPRK00277.

Enzyme and pathway databases

BioCycSAVE227882:SAV5447-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
[Tree]
InterProIPR023562. Pept_S14/S49.
IPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
KOK01358.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP3_STRAW
AccessionPrimary (citable) accession number: Q82CA6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families