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Reviewed, UniProtKB/Swiss-Prot P54415 (CLPP1_SYNE7)

Last modified September 22, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP-dependent Clp protease proteolytic subunit 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1
Gene names
Name: clpP1
Ordered Locus Names: Synpcc7942_1554
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechococcus

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 MF_00444

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase S14 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179686

Sites

Active site961 By similarity
Active site1211 By similarity

Sequences

Sequence LengthMass (Da)Tools
P54415-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: FB9B988AE083751D

FASTA19721,696
        10         20         30         40         50         60 
MIPIVVEESG RGERAFDIYS RLLRERIIFL GEPVTSDVAN RIVAQLLFLE AEDPEKDIYL 

        70         80         90        100        110        120 
YINSPGGSVY DGLGIFDTMN HIRPDVSTVC VGLAASMGAF LLAAGAKGKR TSLAHSRIMI 

       130        140        150        160        170        180 
HQPLGGAQGQ AKDIEIQANE ILYIKQNLNE VLAERTGQPL SRIEDDTDRD FFMSASEAVE 

       190 
YGLIDRVIDR RALKATA 

« Hide

References

« Hide 'large scale' references
[1]"Inactivation of the clpP1 gene for the proteolytic subunit of the ATP-dependent Clp protease in the cyanobacterium Synechococcus limits growth and light acclimation."
Clarke A.K., Schelin J., Porankiewicz J.
Plant Mol. Biol. 37:791-801(1998) [PubMed: 9678574] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

U16135 Genomic DNA. Translation: AAC67306.1.
CP000100 Genomic DNA. Translation: ABB57584.1.
RefSeqYP_400571.1.

3D structure databases

HSSPHSSP built from PDB template 1TYF based on UniProtKB P19245.
ModBaseSearch...

Protein-protein interaction databases

STRINGP54415.

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID3774978.
GenomeReviewsGene locus Synpcc7942_1554 in contig CP000100_GR.
KEGGsyf:Synpcc7942_1554.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP54415.

Enzyme and pathway databases

BioCycMetaCyc:SYNPCC7942_1554-MON.
SELO1140:SYNPCC7942_1554-MON.
BRENDA3.4.21.92. 2064.

Family and domain databases

HAMAPMF_00444.
[Tree]
InterProIPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
PANTHERPTHR10381. Pept_S14_ClpP. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_SYNE7
AccessionPrimary (citable) accession number: P54415
Secondary accession number(s): Q31MY5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 22, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents