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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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).UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei98NucleophileUniRule annotation1
Active sitei123UniRule annotation1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • serine-type endopeptidase activity Source: InterPro

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS14.001.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease proteolytic subunitUniRule annotation (EC:3.4.21.92UniRule annotation)
Alternative name(s):
Endopeptidase ClpUniRule annotation
Gene namesi
Name:clpPUniRule annotation
Ordered Locus Names:MW0730
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000418 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001796541 – 195ATP-dependent Clp protease proteolytic subunitAdd BLAST195

Proteomic databases

PRIDEiP63786.

Interactioni

Subunit structurei

Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-5260070,EBI-5260070

GO - Molecular functioni

  • identical protein binding Source: IntAct

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi15 – 19Combined sources5
Helixi20 – 25Combined sources6
Turni26 – 28Combined sources3
Beta strandi29 – 32Combined sources4
Helixi38 – 54Combined sources17
Beta strandi56 – 58Combined sources3
Beta strandi60 – 66Combined sources7
Helixi71 – 83Combined sources13
Beta strandi84 – 86Combined sources3
Beta strandi88 – 97Combined sources10
Helixi99 – 104Combined sources6
Beta strandi112 – 114Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi126 – 132Combined sources7
Helixi133 – 158Combined sources26
Helixi162 – 168Combined sources7
Beta strandi173 – 176Combined sources4
Helixi177 – 182Combined sources6
Beta strandi187 – 189Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ST9X-ray2.43A/B/C/D/E/F/G1-195[»]
3STAX-ray2.28A/B/C/E/F/G/I/K/L/M/N/S/T/V1-195[»]
4EMMX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/V1-195[»]
4EMPX-ray2.70A/B/C/E/F/G/I/K/L/M/N/S/T/V1-195[»]
ProteinModelPortaliP63786.
SMRiP63786.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63786.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000285833.
KOiK01358.
OMAiGIFDTMQ.

Family and domain databases

CDDicd07017. S14_ClpP_2. 1 hit.
HAMAPiMF_00444. ClpP. 1 hit.
InterProiView protein in InterPro
IPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
IPR018215. ClpP_Ser_AS.
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiView protein in Pfam
PF00574. CLP_protease. 1 hit.
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00493. clpP. 1 hit.
PROSITEiView protein in PROSITE
PS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.

Sequencei

Sequence statusi: Complete.

P63786-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLIPTVIET TNRGERAYDI YSRLLKDRII MLGSQIDDNV ANSIVSQLLF
60 70 80 90 100
LQAQDSEKDI YLYINSPGGS VTAGFAIYDT IQHIKPDVQT ICIGMAASMG
110 120 130 140 150
SFLLAAGAKG KRFALPNAEV MIHQPLGGAQ GQATEIEIAA NHILKTREKL
160 170 180 190
NRILSERTGQ SIEKIQKDTD RDNFLTAEEA KEYGLIDEVM VPETK
Length:195
Mass (Da):21,514
Last modified:October 11, 2004 - v1
Checksum:i811110E32846625E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94595.1.
RefSeqiWP_001049165.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94595; BAB94595; BAB94595.
GeneIDi31213584.
KEGGisam:MW0730.

Similar proteinsi

Entry informationi

Entry nameiCLPP_STAAW
AccessioniPrimary (citable) accession number: P63786
Secondary accession number(s): Q99VK9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: September 27, 2017
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families