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Q6A7F0 (CLPP1_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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 1

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp 1
Gene names
Name:clpP1
Ordered Locus Names:PPA1572
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length216 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.

Sequence caution

The sequence AAT83315.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-KW

   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179615

Sites

Active site1191 By similarity
Active site1441 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6A7F0 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: DD163019628122CF

FASTA21623,589
        10         20         30         40         50         60 
MNAEQAEQAA PGGLAPAGPR NDYYIPQWEE RTSYGVRRVD PYTKLFEDRI IFLGTPVTDD 

        70         80         90        100        110        120 
IANAVMAQLL CLQSMDADRQ ISMYINSPGG SFTAMTAIYD TMNYVRPDIQ TICLGMAASA 

       130        140        150        160        170        180 
AAVLLAAGAK GQRLSLPNST VLIHQPAMGQ ATYGQATDIE ILDDEIQRIR KLMENMLATA 

       190        200        210 
TGQSVEQISK DIDRDKYLTA QGAKEYGLID DILTSL 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT83315.1. Different initiation.
RefSeqYP_056273.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A7F0.
SMRQ6A7F0. Positions 34-215.
ModBaseSearch...

Protein family/group databases

MEROPSS14.009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2931005.
GenomeReviewsGene locus PPA1572 in contig AE017283_GR.
KEGGpac:PPA1572.
NMPDRfig|267747.1.peg.1550.
PATRIC23037919. VBIProAcn64440_1618.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG558421.
OMAQDPYTKL.
ProtClustDBCLSK2764058.

Enzyme and pathway databases

BioCycPACN267747:PPA1572-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
[Tree]
InterProIPR023562. Pept_S14/S49.
IPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
KOK01358.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_PROAC
AccessionPrimary (citable) accession number: Q6A7F0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families