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Reviewed, UniProtKB/Swiss-Prot Q6ME32 (CLPP1_PARUW)

Last modified January 19, 2010. Version 40. 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: pc0443
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

Protein attributes

Sequence length206 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 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 MF_00444

Subcellular location

Cytoplasm By similarity HAMAP MF_00444.

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 – 206206ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179608

Sites

Active site1031 By similarity
Active site1281 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ME32-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: C49FD35760BFD85B

FASTA20622,617
        10         20         30         40         50         60 
MTRETSMPKH DKNKSAIPSK MADRIEHAIL DSRRIFISDA VDSGSASEII RKLWYLELTD 

        70         80         90        100        110        120 
PGKPILFVIN SPGGAVDSGF AIWDQIKMIT SPVTTLVTGL AASMGSILSL CASPGRRFAT 

       130        140        150        160        170        180 
PHSRIMIHQP LLSGVIKGQA TDLEIQAKEM LKTRNGLIEI YVQATGKNFA AIEKAIDRDT 

       190        200 
WMTAQEALEF GLLDKVINSF EEIEST 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed: 15073324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF23167.1.
RefSeqYP_007442.1.

3D structure databases

SMRQ6ME32. Positions 22-201.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6ME32.

Protein family/group databases

MEROPSS14.005.

Genome annotation databases

GeneID2780284.
GenomeReviewsGene locus pc0443 in contig BX908798_GR.
KEGGpcu:pc0443.
NMPDRfig|264201.1.peg.443.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHBG558421.
OMATPHSRIM.

Enzyme and pathway databases

BioCycCPRO264201:PC0443-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
[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.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_PARUW
AccessionPrimary (citable) accession number: Q6ME32
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: January 19, 2010
This is version 40 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