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Q8NN01 (CLPP2_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. 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:Cgl2412, cg2645
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence caution

The sequence CAF21076.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical termComplete proteome
Reference 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 – 201201ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000179546

Sites

Active site1001 By similarity
Active site1251 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NN01 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: C20B7C879FB3372F

FASTA20121,630
        10         20         30         40         50         60 
MTVFMSDIRM AAQGGPGFGN DVFDRLLSER IIFLGSQVDD EIANKLCAQI LLLSAEDPTR 

        70         80         90        100        110        120 
DISLYINSPG GSVTAGMAIY DTMKYSPCDI ATYGMGLAAS MGQFLLSGGT KGKRFALPHA 

       130        140        150        160        170        180 
RIMMHQPSAG VGGTAADIAI QAEQFAATKR EMAQLIAEHT GQTFEQISKD SDRDRWFTAQ 

       190        200 
EAKDYGLVDH VITLAEGPIS N 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99805.1.
BX927155 Genomic DNA. Translation: CAF21076.1. Different initiation.
RefSeqNP_601612.1. NC_003450.3.
YP_226656.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NN01.
SMRQ8NN01. Positions 20-195.
ModBaseSearch...

Protein family/group databases

MEROPSS14.008.

2D gel databases

World-2DPAGE0001:Q8NN01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1020361.
3345290.
GenomeReviewsGene locus Cgl2412 in contig BA000036_GR.
Gene locus cg2645 in contig BX927147_GR.
KEGGcgb:cg2645.
cgl:NCgl2328.
PATRIC21496828. VBICorGlu203724_2346.

Phylogenomic databases

HOGENOMHBG558421.
OMACDIATYG.
ProtClustDBPRK00277.

Enzyme and pathway databases

BioCycCGLU196627:CG2645-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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP2_CORGL
AccessionPrimary (citable) accession number: Q8NN01
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 58 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