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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
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 sitei101NucleophileUniRule annotation1
Active sitei126UniRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

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:FTT_0624
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001795581 – 201ATP-dependent Clp protease proteolytic subunitAdd BLAST201

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

IntActiQ5NH47. 1 interactor.
STRINGi177416.FTT_0624.

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Helixi23 – 29Combined sources7
Beta strandi32 – 37Combined sources6
Helixi41 – 57Combined sources17
Beta strandi59 – 61Combined sources3
Beta strandi63 – 69Combined sources7
Helixi74 – 86Combined sources13
Beta strandi87 – 89Combined sources3
Beta strandi91 – 100Combined sources10
Helixi102 – 108Combined sources7
Beta strandi115 – 117Combined sources3
Beta strandi122 – 125Combined sources4
Beta strandi129 – 135Combined sources7
Helixi136 – 161Combined sources26
Helixi165 – 171Combined sources7
Beta strandi176 – 179Combined sources4
Helixi180 – 186Combined sources7
Beta strandi190 – 192Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P2LX-ray2.30A/B/C/D/E/F/G4-201[»]
5G1QX-ray2.84A/B/C/D/E/F/G1-201[»]
5G1RX-ray1.90A/B/C/D/E/F/G1-201[»]
5G1SX-ray1.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U1-201[»]
ProteinModelPortaliQ5NH47.
SMRiQ5NH47.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5NH47.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
KOiK01358.
OMAiARMNELM.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP. 1 hit.
InterProiIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
IPR018215. ClpP_Ser_AS.
[Graphical view]
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00493. clpP. 1 hit.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5NH47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITNNLVPTV IEKTAGGERA FDIYSRLLKE RIVFLNGEVN DHSANLVIAQ
60 70 80 90 100
LLFLESEDPD KDIYFYINSP GGMVTAGMGV YDTMQFIKPD VSTICIGLAA
110 120 130 140 150
SMGSLLLAGG AKGKRYSLPS SQIMIHQPLG GFRGQASDIE IHAKNILRIK
160 170 180 190 200
DRLNKVLAHH TGQDLETIVK DTDRDNFMMA DEAKAYGLID HVIESREAII

K
Length:201
Mass (Da):22,150
Last modified:February 1, 2005 - v1
Checksum:iCE00A6E52FC18FD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45257.1.
RefSeqiWP_003015534.1. NZ_CP010290.1.
YP_169645.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45257; CAG45257; FTT_0624.
GeneIDi3192361.
KEGGiftu:FTT_0624.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45257.1.
RefSeqiWP_003015534.1. NZ_CP010290.1.
YP_169645.1. NC_006570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P2LX-ray2.30A/B/C/D/E/F/G4-201[»]
5G1QX-ray2.84A/B/C/D/E/F/G1-201[»]
5G1RX-ray1.90A/B/C/D/E/F/G1-201[»]
5G1SX-ray1.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U1-201[»]
ProteinModelPortaliQ5NH47.
SMRiQ5NH47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5NH47. 1 interactor.
STRINGi177416.FTT_0624.

Protocols and materials databases

DNASUi3192361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG45257; CAG45257; FTT_0624.
GeneIDi3192361.
KEGGiftu:FTT_0624.

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
KOiK01358.
OMAiARMNELM.

Miscellaneous databases

EvolutionaryTraceiQ5NH47.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP. 1 hit.
InterProiIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
IPR018215. ClpP_Ser_AS.
[Graphical view]
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00493. clpP. 1 hit.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLPP_FRATT
AccessioniPrimary (citable) accession number: Q5NH47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: November 30, 2016
This is version 84 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.