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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed-Annotation score: Annotation score: 2 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 sitei96NucleophileUniRule annotation1
Active sitei121UniRule annotation1

GO - Molecular functioni

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:spr0656
OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
Taxonomic identifieri171101 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000586 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001796711 – 196ATP-dependent Clp protease proteolytic subunitAdd BLAST196

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

STRINGi171101.spr0656.

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 24Combined sources7
Beta strandi27 – 32Combined sources6
Helixi36 – 52Combined sources17
Beta strandi58 – 64Combined sources7
Helixi69 – 81Combined sources13
Beta strandi82 – 84Combined sources3
Beta strandi86 – 95Combined sources10
Helixi97 – 102Combined sources6
Beta strandi110 – 112Combined sources3
Beta strandi117 – 119Combined sources3
Helixi140 – 158Combined sources19
Helixi162 – 170Combined sources9
Helixi177 – 183Combined sources7
Beta strandi187 – 189Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y7OX-ray2.51A/B/C/D/E/F/G1-196[»]
ProteinModelPortaliP63788.
SMRiP63788.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63788.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
KOiK01358.
OMAiLFLQSEN.

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.
PROSITEiView protein in PROSITE
PS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.

Sequencei

Sequence statusi: Complete.

P63788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPVVIEQTS RGERSYDIYS RLLKDRIIML TGPVEDNMAN SVIAQLLFLD
60 70 80 90 100
AQDSTKDIYL YVNTPGGSVS AGLAIVDTMN FIKADVQTIV MGMAASMGTV
110 120 130 140 150
IASSGAKGKR FMLPNAEYMI HQPMGGTGGG TQQTDMAIAA EHLLKTRNTL
160 170 180 190
EKILAENSGQ SMEKVHADAE RDNWMSAQET LEYGFIDEIM ANNSLN
Length:196
Mass (Da):21,358
Last modified:October 11, 2004 - v1
Checksum:i2C6C3A820A290B2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007317 Genomic DNA. Translation: AAK99460.1.
PIRiH97953.
RefSeqiNP_358250.1. NC_003098.1.
WP_000613477.1. NC_003098.1.

Genome annotation databases

EnsemblBacteriaiAAK99460; AAK99460; spr0656.
GeneIDi934194.
KEGGispr:spr0656.
PATRICifig|171101.6.peg.728.

Similar proteinsi

Entry informationi

Entry nameiCLPP_STRR6
AccessioniPrimary (citable) accession number: P63788
Secondary accession number(s): P58279
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: September 27, 2017
This is version 88 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