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Reviewed, UniProtKB/Swiss-Prot Q7VC22 (CLPP1_PROMA)

Last modified February 9, 2010. Version 41. 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 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1
Gene names
Name: clpP1
Ordered Locus Names: Pro_0920
OrganismProchlorococcus marinus [Complete proteome] [HAMAP]
Taxonomic identifier1219 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length196 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: 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 – 196196ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179617

Sites

Active site961 By similarity
Active site1211 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VC22-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 12E104616F09C8C0

FASTA19621,666
        10         20         30         40         50         60 
MIPIVVEETG RGERAFDIYS RLLRERIVFL GEQVTNDSAN RIVAQLLFLE AEDPEKDIFL 

        70         80         90        100        110        120 
YINSPGGSVY DGFGIFDTIQ HIKPDVHTVC VGLAASMGAF LLCAGAKGKR SSLQHSRIMI 

       130        140        150        160        170        180 
HQPLGGARGQ ATDIRIQADE ILFLKQKLNT ELSNRTGQPL SKIAEDTDRD FYMSPSEAIS 

       190 
YGIIDNVLNK KPVSVL 

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References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed: 12917486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAP99964.1.
RefSeqNP_875312.1.

3D structure databases

SMRQ7VC22. Positions 1-191.
ModBaseSearch...

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID1462302.
GenomeReviewsGene locus Pro_0920 in contig AE017126_GR.
KEGGpma:Pro0920.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG558421.
OMADIRIQAD.

Enzyme and pathway databases

BioCycPMAR167539:PRO_0920-MONOMER.
BRENDA3.4.21.92. 141456.

Family and domain databases

HAMAPMF_00444. ClpP.
[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. False negative.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_PROMA
AccessionPrimary (citable) accession number: Q7VC22
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2003
Last modified: February 9, 2010
This is version 41 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