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Q48KZ0 (CLPP_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp
Gene names
Name:clpP
Ordered Locus Names:PSPPH_1698
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00444

Catalytic activity

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). HAMAP-Rule MF_00444

Subunit structure

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.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00444.

Sequence similarities

Belongs to the peptidase S14 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Serine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213ATP-dependent Clp protease proteolytic subunit HAMAP-Rule MF_00444
PRO_0000226461

Sites

Active site1141Nucleophile By similarity
Active site1391 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48KZ0 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 46D77E6981A5B206

FASTA21323,578
        10         20         30         40         50         60 
MSRNSYIQQN SDIQAAGGLV PMVIEQSARG ERAYDIYSRL LKERVIFMVG PVEDYMANLI 

        70         80         90        100        110        120 
AAQLLFLEAE NPDKDIHLYI NSPGGSVTAG MSIYDTMQFI KPDVSTICIG QACSMGAFLL 

       130        140        150        160        170        180 
AGGAEGKRHC LPNSRMMIHQ PLGGFQGQAS DIDIHAKEIL HIRHRLNSLL AHHTGQSLET 

       190        200        210 
IERDTERDNF MSAERAAEYG LIDSVINKRQ MPA 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ33449.1.
RefSeqYP_273935.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48KZ0.
SMRQ48KZ0. Positions 19-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_1698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ33449; AAZ33449; PSPPH_1698.
GeneID3555975.
KEGGpsp:PSPPH_1698.
PATRIC19972571. VBIPseSyr78478_1781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHOG000285833.
KOK01358.
OMAKGERSFD.
OrthoDBEOG6Z3KQ0.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-1701-MONOMER.

Family and domain databases

Gene3D3.90.226.10. 1 hit.
HAMAPMF_00444. ClpP.
InterProIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR018215. ClpP_AS.
[Graphical view]
PANTHERPTHR10381. PTHR10381. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
SUPFAMSSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP_PSE14
AccessionPrimary (citable) accession number: Q48KZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries