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Reviewed, UniProtKB/Swiss-Prot Q3MDK7 (CLPP2_ANAVT)

Last modified June 16, 2009. Version 24. 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: Ava_1305
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

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 2 HAMAP MF_00444
PRO_0000236380

Sites

Active site1011 By similarity
Active site1261 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MDK7-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 42DE88ED2880B853

FASTA19722,205
        10         20         30         40         50         60 
MPIGVPKVPY RMPGGQFTDW ISIYDRLYRE RIIFLGRDVD DEIANQIIAV MLYLDSEDPG 

        70         80         90        100        110        120 
KDIYLYINSP GGMVTSGLAI YDTMQHIKSD VVTICVGLAA SMGSFLLAAG TKGKRLALPH 

       130        140        150        160        170        180 
SRIMIHQPSG GTRGQATDIE IEAREILRIR HQLNQIYANN TNQPLAKIEK DMDRDFFMSA 

       190 
QEAKEYGLID RVIEERI 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000117 Genomic DNA. Translation: ABA20929.1.
RefSeqYP_321824.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID3683048.
GenomeReviewsGene locus Ava_1305 in contig CP000117_GR.
KEGGava:Ava_1305.
NMPDRfig|240292.3.peg.2150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3MDK7.
OMAQ3MDK7. DGVANSL.

Enzyme and pathway databases

BioCycAVAR240292:AVA_1305-MON.

Family and domain databases

HAMAPMF_00444.
[Tree]
InterProIPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_CS.
[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_ANAVT
AccessionPrimary (citable) accession number: Q3MDK7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 25, 2005
Last modified: June 16, 2009
This is version 24 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