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Q24S49 (CLPP2_DESHY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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 2

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp 2
Gene names
Name:clpP2
Ordered Locus Names:DSY3354
OrganismDesulfitobacterium hafniense (strain Y51) [Complete proteome] [HAMAP]
Taxonomic identifier138119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

Protein attributes

Sequence length202 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: 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 – 202202ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000252815

Sites

Active site991 By similarity
Active site1241 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q24S49 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 881CFDDA0D760FF6

FASTA20222,421
        10         20         30         40         50         60 
MSYLVPMVIE QTNRGERSYD IYSRLLKDRI IFLGGPVTDD VANLVVAQML FLEAEDPEKD 

        70         80         90        100        110        120 
IFLYINSPGG SISAGMAIYD TMQYIRADVH TICVGLAASM GAFLLTAGAK GKRQALPNAE 

       130        140        150        160        170        180 
ILIHQPLIGG GGISGQATEI EIHAKHLLRV KERMNRILAE RTGQTIERIE ADTDRDRYMT 

       190        200 
AEEAKEYGLI DEVLEKPNQP KK 

« Hide

References

[1]"Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195."
Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., Inatomi K., Furukawa K., Inui M., Yukawa H.
J. Bacteriol. 188:2262-2274(2006) [PubMed: 16513756] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008230 Genomic DNA. Translation: BAE85143.1.
RefSeqYP_519587.1. NC_007907.1.

3D structure databases

HSSPHSSP built from PDB template 2FZS based on UniProtKB P0A6G7.
ProteinModelPortalQ24S49.
SMRQ24S49. Positions 4-198.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ24S49.

Protein family/group databases

MEROPSS14.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3954529.
GenomeReviewsGene locus DSY3354 in contig AP008230_GR.
KEGGdsy:DSY3354.
NMPDRfig|138119.3.peg.4671.
PATRIC21675626. VBIDesHaf65307_3741.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHBG558421.
OMAELMAKHT.
PhylomeDBQ24S49.
ProtClustDBCLSK2466684.

Enzyme and pathway databases

BioCycDHAF138119:DSY3354-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.
TIGRFAMsTIGR00493. ClpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP2_DESHY
AccessionPrimary (citable) accession number: Q24S49
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 18, 2006
Last modified: January 25, 2012
This is version 43 of the entry and version 1 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