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Reviewed, UniProtKB/Swiss-Prot Q5L4W7 (CLPP2_CHLAB)

Last modified November 3, 2009. Version 27. 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 2
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 2
Gene names
Name: clpP2
Ordered Locus Names: CAB888
OrganismChlamydophila abortus [Complete proteome] [HAMAP]
Taxonomic identifier83555 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydophila

Protein attributes

Sequence length205 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 – 205205ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000226438

Sites

Active site1001 By similarity
Active site1251 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L4W7-1 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 471875055009135F

FASTA20522,364
        10         20         30         40         50         60 
MQMTLVPYVV EDTGRGERAM DIYSRLLKDR IVMIGQEITE PLANTVIAQL LFLMSEDPKK 

        70         80         90        100        110        120 
DIKVFINSPG GYITAGLAIY DTIRFLGCDV NTYCIGQAAS MGALLLSAGT KGKRYALPHS 

       130        140        150        160        170        180 
RMMIHQPSGG IIGTSADIQL QAAEILTLKK HLANILSECT GQPVEKIIED SERDFFMGAE 

       190        200 
DAISYGLIDK VVSSAKDTKD KDTIS 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed: 15837807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S26/3.

Cross-references

Sequence databases

CR848038 Genomic DNA. Translation: CAH64328.1.
RefSeqYP_220275.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID3337633.
GenomeReviewsGene locus CAB888 in contig CR848038_GR.
KEGGcab:CAB888.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5L4W7.
OMAANKLCAQ.

Enzyme and pathway databases

BioCycCABO218497:CAB888-MON.
BRENDA3.4.21.92. 292247.

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.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP2_CHLAB
AccessionPrimary (citable) accession number: Q5L4W7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: June 21, 2005
Last modified: November 3, 2009
This is version 27 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