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Reviewed, UniProtKB/Swiss-Prot Q8FN37 (CLPP1_COREF)

Last modified January 19, 2010. 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 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1
Gene names
Name: clpP1
Ordered Locus Names: CE2311
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length208 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 – 208208ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179543

Sites

Active site1081 By similarity
Active site1331 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FN37-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 08C936D334CAFA73

FASTA20822,883
        10         20         30         40         50         60 
MSNGFQMPSS RYVLPSFIEQ SAYGTKETNP YAKLFEERII FLGTQVDDTS ANDIMAQLLV 

        70         80         90        100        110        120 
LEGMDPDRDI TMYINSPGGS FTALMAIYDT MQYVRPDVQT VCLGQAASAA AVLLAAGAPG 

       130        140        150        160        170        180 
KRAALPNARV LIHQPATQGT QGQVSDLEIQ AAEIERMRKL METTLSQHTG KTPEQIRIDT 

       190        200 
DRDKILTAEG ALEYGIIDQV FDYRKLNT 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC19121.1.
RefSeqNP_738921.1.

3D structure databases

SMRQ8FN37. Positions 29-205.
ModBaseSearch...

Protein family/group databases

MEROPSS14.009.

Genome annotation databases

GeneID1034826.
GenomeReviewsGene locus CE2311 in contig BA000035_GR.
KEGGcef:CE2311.
NMPDRfig|196164.1.peg.2311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG558421.
OMARKLSAQK.

Enzyme and pathway databases

BioCycCEFF196164:CE2311-MONOMER.
BRENDA3.4.21.92. 277326.

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

Entry information

Entry nameCLPP1_COREF
AccessionPrimary (citable) accession number: Q8FN37
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: January 19, 2010
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