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Protein

ATP-dependent Clp protease proteolytic subunit, mitochondrial

Gene

CLPP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates (By similarity).By similarity

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 1491NucleophileBy similarity
Active sitei174 – 1741By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS14.003.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC:3.4.21.92)
Alternative name(s):
Endopeptidase Clp
Gene namesi
Name:CLPP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 272ATP-dependent Clp protease proteolytic subunit, mitochondrialPRO_0000260318
Transit peptidei1 – 5252MitochondrionBy similarityAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-succinyllysineBy similarity
Modified residuei207 – 2071N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ2KHU4.
PeptideAtlasiQ2KHU4.
PRIDEiQ2KHU4.

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. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019577.

Structurei

3D structure databases

ProteinModelPortaliQ2KHU4.
SMRiQ2KHU4. Positions 53-257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0840. Eukaryota.
COG0740. LUCA.
GeneTreeiENSGT00390000005830.
HOGENOMiHOG000285833.
HOVERGENiHBG001689.
InParanoidiQ2KHU4.
KOiK01358.
OMAiARMNELM.
OrthoDBiEOG77WWD5.
TreeFamiTF105002.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP.
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.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2KHU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWPKILLRGG RVAAGLCPAL GPRLAARFPP QRTPENRLAP QRNLHATAAR
60 70 80 90 100
ALPLIPIVVE QTGRGERAYD IYSRLLRERI VCVMGPIDDS VASLVIAQLL
110 120 130 140 150
FLQSESNKKP IHMYINSPGG VVTSGLAIYD TMQYILNPIC TWCVGQAASM
160 170 180 190 200
GSLLLAAGTP GMRHSLPNSR IMIHQPSGGA RGQATDIAIQ AEEIMKLKKQ
210 220 230 240 250
LYSIYAKHTK QSLQVIESAM ERDRYMSPME AQEFGILDKV LVHPPQDGED
260 270
EPELVQKEPG EPTAVEPAPA SA
Length:272
Mass (Da):29,704
Last modified:March 7, 2006 - v1
Checksum:i093E2BF04EA98EDC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112880 mRNA. Translation: AAI12881.1.
RefSeqiNP_001039879.1. NM_001046414.2.
UniGeneiBt.54443.

Genome annotation databases

EnsembliENSBTAT00000019577; ENSBTAP00000019577; ENSBTAG00000014712.
GeneIDi535981.
KEGGibta:535981.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112880 mRNA. Translation: AAI12881.1.
RefSeqiNP_001039879.1. NM_001046414.2.
UniGeneiBt.54443.

3D structure databases

ProteinModelPortaliQ2KHU4.
SMRiQ2KHU4. Positions 53-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019577.

Protein family/group databases

MEROPSiS14.003.

Proteomic databases

PaxDbiQ2KHU4.
PeptideAtlasiQ2KHU4.
PRIDEiQ2KHU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000019577; ENSBTAP00000019577; ENSBTAG00000014712.
GeneIDi535981.
KEGGibta:535981.

Organism-specific databases

CTDi8192.

Phylogenomic databases

eggNOGiKOG0840. Eukaryota.
COG0740. LUCA.
GeneTreeiENSGT00390000005830.
HOGENOMiHOG000285833.
HOVERGENiHBG001689.
InParanoidiQ2KHU4.
KOiK01358.
OMAiARMNELM.
OrthoDBiEOG77WWD5.
TreeFamiTF105002.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP.
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.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Heart ventricle.

Entry informationi

Entry nameiCLPP_BOVIN
AccessioniPrimary (citable) accession number: Q2KHU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 7, 2006
Last modified: July 6, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.