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Q4FQB9 (CLPP_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp
Gene names
Name:clpP
Ordered Locus Names:Psyc_1941
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length225 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-Rule 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-Rule MF_00444

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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-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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225ATP-dependent Clp protease proteolytic subunit HAMAP-Rule MF_00444
PRO_0000226463

Sites

Active site1261 By similarity
Active site1511 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FQB9 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: EFB0E14A3617304C

FASTA22525,056
        10         20         30         40         50         60 
MTDYDRITAN PHFDMLMSAH NHVQSTTQSA LVPMVVEQSA RGERSFDIFS RLLRERVIFL 

        70         80         90        100        110        120 
TGQVEDHMAN LIVAQLLFLE AENPDKDIHL YINSPGGSVS AGLAIFDTMN FIKPEVSTIC 

       130        140        150        160        170        180 
MGGAYSMGSF LLAAGQKGKR YALANARVMI HQPSGGAQGQ ATDIEINARE ILKTRARLNE 

       190        200        210        220 
ILAERTGQSV EKIEKDVERD YWLDAKEAKE YGLIDEVLER RPASL 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ19789.1.
RefSeqYP_265223.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FQB9.
SMRQ4FQB9. Positions 30-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_1941.

Protein family/group databases

MEROPSS14.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ19789; AAZ19789; Psyc_1941.
GeneID3515911.
KEGGpar:Psyc_1941.
PATRIC23058779. VBIPsyArc98534_2294.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHOG000285833.
KOK01358.
OMAERDYWMD.
OrthoDBEOG6Z3KQ0.
ProtClustDBPRK00277.

Enzyme and pathway databases

BioCycPARC259536:GI3A-1986-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
InterProIPR001907. ClpP.
IPR023562. ClpP/TepA.
IPR018215. ClpP_AS.
[Graphical view]
PANTHERPTHR10381. PTHR10381. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP_PSYA2
AccessionPrimary (citable) accession number: Q4FQB9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: August 30, 2005
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries