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Reviewed, UniProtKB/Swiss-Prot Q8YQX8 (CLPP2_ANASP)

Last modified November 3, 2009. Version 42. 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: alr3683
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length232 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 – 232232ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000179479

Sites

Active site1241 By similarity
Active site1491 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YQX8-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 1C138C7A7B99D2A1

FASTA23225,341
        10         20         30         40         50         60 
MLVSQSANHS INSLSRFGMS SHLNGIGNIV PMVVEQSGMG ERAFDIYSRL LRERIIFLGT 

        70         80         90        100        110        120 
PIDDAVANTI VAQLLFLDAE DSEKDIQLYI NSPGGSVYAG MAIYDTIQQI RPDVVTICFG 

       130        140        150        160        170        180 
LAASMGAFLL TAGTKGKRMS LPDSRIMIHQ PLGGAQGQAI DIEIQAREIL YIKAQLNQLL 

       190        200        210        220        230 
ANHTGQPLER IEADTDRDFF MSAEEAKNYG LIDQVISRQN LPTAGENVTI VK 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000019 Genomic DNA. Translation: BAB75382.1.
PIRAD2266.
RefSeqNP_487723.1.

3D structure databases

HSSPHSSP built from PDB template 1TYF based on UniProtKB P19245.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YQX8.

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID1107281.
GenomeReviewsGene locus alr3683 in contig BA000019_GR.
KEGGana:alr3683.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8YQX8.
OMAVEQTAKG.

Enzyme and pathway databases

BioCycNSP103690:ALR3683-MON.

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.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP2_ANASP
AccessionPrimary (citable) accession number: Q8YQX8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: March 1, 2002
Last modified: November 3, 2009
This is version 42 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