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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCyciSAUR93061:G1G5Y-740-MONOMER

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:SAOUHSC_00790
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1932910

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002528511 – 195ATP-dependent Clp protease proteolytic subunitAdd BLAST195

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

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00790

Chemistry databases

BindingDBiQ2G036

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi17 – 19Combined sources3
Helixi20 – 26Combined sources7
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 – 105Combined sources7
Beta strandi112 – 114Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi126 – 132Combined sources7
Helixi133 – 158Combined sources26
Helixi162 – 168Combined sources7
Beta strandi173 – 176Combined sources4
Helixi177 – 183Combined sources7
Beta strandi187 – 189Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QWDX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N1-195[»]
3V5EX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N1-195[»]
3V5IX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b1-195[»]
4MXIX-ray2.30A/B/C/D/E/F/G1-195[»]
5C90X-ray1.75A/B/C/D/E/F/G/H/I/J/K/L/M/N1-195[»]
5VZ2X-ray2.26A/B/C/D/E/F/G/I/K/L/M/N/S/T1-195[»]
5W18X-ray2.44A/B/C/D/E/F/G/I/K/L/M/N/S/T1-195[»]
ProteinModelPortaliQ2G036
SMRiQ2G036
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2G036

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCQ Bacteria
COG0740 LUCA
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_sf
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.

Q2G036-1 [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:March 21, 2006 - v1
Checksum:i811110E32846625E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000253 Genomic DNA Translation: ABD29919.1
RefSeqiWP_001049165.1, NC_007795.1
YP_499347.1, NC_007795.1

Genome annotation databases

EnsemblBacteriaiABD29919; ABD29919; SAOUHSC_00790
GeneIDi3919354
KEGGisao:SAOUHSC_00790
PATRICifig|93061.5.peg.713

Similar proteinsi

Entry informationi

Entry nameiCLPP_STAA8
AccessioniPrimary (citable) accession number: Q2G036
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 21, 2006
Last modified: March 28, 2018
This is version 86 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, Reference 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
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Main funding by: National Institutes of Health