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Q7V8M4 (CLPP2_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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 2

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp 2
Gene names
Name:clpP2
Ordered Locus Names:PMT_0314
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length200 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: UniProtKB-KW

   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000179621

Sites

Active site1011 By similarity
Active site1261 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V8M4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 46A5CE4E45F47BD2

FASTA20022,024
        10         20         30         40         50         60 
MPIGTPSVPY RLPGSQMERW VDIYTRLGVE RILFLGQEVS DGVANSLVAQ MLYLDSEDST 

        70         80         90        100        110        120 
KPIYLYINSP GGSVTAGLAI YDTMKYVKSD VVTICVGLAA SMGAFLLTAG TKGKRLALPH 

       130        140        150        160        170        180 
SRIMIHQPLG GTNQRQASDI EIEAREILRI KDMLNHSMAE LTGQSFEKIE KDTDRDYFLS 

       190        200 
AAEAKDYGLI DRVIAHPNEA 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20489.1.
RefSeqNP_894147.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V8M4.
SMRQ7V8M4. Positions 15-198.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V8M4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1729785.
GenomeReviewsGene locus PMT_0314 in contig BX548175_GR.
KEGGpmt:PMT0314.
NMPDRfig|74547.1.peg.314.
PATRIC23008421. VBIProMar135351_0371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHBG558421.
OMADGVANSL.
PhylomeDBQ7V8M4.
ProtClustDBPRK00277.

Enzyme and pathway databases

BioCycPMAR74547:PMT0314-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
[Tree]
InterProIPR023562. Pept_S14/S49.
IPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
KOK01358.
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_PROMM
AccessionPrimary (citable) accession number: Q7V8M4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families