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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (PubMed:16899079). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451).UniRule annotation2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981NucleophileUniRule annotation
Active sitei123 – 1231UniRule annotation

GO - Molecular functioni

  • ATP-dependent peptidase activity Source: CACAO
  • serine-type endopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciBSUB:BSU34540-MONOMER.
BRENDAi3.4.21.92. 658.

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):
Caseinolytic protease
Endopeptidase ClpUniRule annotation
Stress protein G7
Gene namesi
Name:clpPUniRule annotation
Synonyms:yvdN
Ordered Locus Names:BSU34540
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No degradation of trans-translationally tagged-peptides.1 Publication

Chemistry

ChEMBLiCHEMBL2146309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197ATP-dependent Clp protease proteolytic subunitPRO_0000179501Add
BLAST

Proteomic databases

PaxDbiP80244.
PRIDEiP80244.

Expressioni

Inductioni

By heat shock, salt stress, ethanol stress, oxidative stress, glucose limitation and oxygen limitation.3 Publications

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 (By similarity). Forms large heterooligomeric complexes consisting of an ATPase component (ClpX, ClpC or ClpE) and a proteolytic component (ClpP).UniRule annotation

Protein-protein interaction databases

DIPiDIP-43711N.
IntActiP80244. 1 interaction.
MINTiMINT-2838977.
STRINGi224308.Bsubs1_010100018711.

Structurei

Secondary structure

1
197
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 267Combined sources
Beta strandi29 – 324Combined sources
Helixi38 – 5417Combined sources
Beta strandi56 – 583Combined sources
Beta strandi60 – 667Combined sources
Helixi71 – 8313Combined sources
Beta strandi84 – 863Combined sources
Beta strandi88 – 9710Combined sources
Helixi99 – 1057Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi126 – 1327Combined sources
Helixi133 – 15826Combined sources
Helixi162 – 1687Combined sources
Beta strandi173 – 1764Combined sources
Helixi177 – 1837Combined sources
Beta strandi187 – 1893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KTGX-ray2.40A/B/C/D/E/F/G2-197[»]
3KTHX-ray3.00A/B/C/D/E/F/G2-197[»]
3KTIX-ray2.00A/B/C/D/E/F/G2-197[»]
3KTJX-ray2.60A/B/C/D/E/F/G2-197[»]
3KTKX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N2-197[»]
3TT6X-ray2.59A/B/C/D/E/F/G2-197[»]
3TT7X-ray2.56A/B/C/D/E/F/G1-197[»]
ProteinModelPortaliP80244.
SMRiP80244. Positions 19-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80244.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
InParanoidiP80244.
KOiK01358.
OMAiARMNELM.
PhylomeDBiP80244.

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.

P80244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLIPTVIEQ TNRGERAYDI YSRLLKDRII MLGSAIDDNV ANSIVSQLLF
60 70 80 90 100
LAAEDPEKEI SLYINSPGGS ITAGMAIYDT MQFIKPKVST ICIGMAASMG
110 120 130 140 150
AFLLAAGEKG KRYALPNSEV MIHQPLGGAQ GQATEIEIAA KRILLLRDKL
160 170 180 190
NKVLAERTGQ PLEVIERDTD RDNFKSAEEA LEYGLIDKIL THTEDKK
Length:197
Mass (Da):21,682
Last modified:July 15, 1998 - v3
Checksum:i5D4D4BD548DC45A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59754 Genomic DNA. Translation: AAC46381.1.
Z94043 Genomic DNA. Translation: CAB08043.1.
AL009126 Genomic DNA. Translation: CAB15459.1.
PIRiB69601.
RefSeqiNP_391334.1. NC_000964.3.
WP_003228214.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15459; CAB15459; BSU34540.
GeneIDi938625.
KEGGibsu:BSU34540.
PATRICi18978912. VBIBacSub10457_3618.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59754 Genomic DNA. Translation: AAC46381.1.
Z94043 Genomic DNA. Translation: CAB08043.1.
AL009126 Genomic DNA. Translation: CAB15459.1.
PIRiB69601.
RefSeqiNP_391334.1. NC_000964.3.
WP_003228214.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KTGX-ray2.40A/B/C/D/E/F/G2-197[»]
3KTHX-ray3.00A/B/C/D/E/F/G2-197[»]
3KTIX-ray2.00A/B/C/D/E/F/G2-197[»]
3KTJX-ray2.60A/B/C/D/E/F/G2-197[»]
3KTKX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N2-197[»]
3TT6X-ray2.59A/B/C/D/E/F/G2-197[»]
3TT7X-ray2.56A/B/C/D/E/F/G1-197[»]
ProteinModelPortaliP80244.
SMRiP80244. Positions 19-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-43711N.
IntActiP80244. 1 interaction.
MINTiMINT-2838977.
STRINGi224308.Bsubs1_010100018711.

Chemistry

ChEMBLiCHEMBL2146309.

Protein family/group databases

MEROPSiS14.001.

Proteomic databases

PaxDbiP80244.
PRIDEiP80244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15459; CAB15459; BSU34540.
GeneIDi938625.
KEGGibsu:BSU34540.
PATRICi18978912. VBIBacSub10457_3618.

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
InParanoidiP80244.
KOiK01358.
OMAiARMNELM.
PhylomeDBiP80244.

Enzyme and pathway databases

BioCyciBSUB:BSU34540-MONOMER.
BRENDAi3.4.21.92. 658.

Miscellaneous databases

EvolutionaryTraceiP80244.

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_BACSU
AccessioniPrimary (citable) accession number: P80244
Secondary accession number(s): O08433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: September 7, 2016
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.