Q8NN02 (CLPP1_CORGL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: ATP-dependent Clp protease proteolytic subunit 1 EC=3.4.21.92 Alternative name(s): Endopeptidase Clp 1 | ||||
| Gene names |
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| Organism | Corynebacterium glutamicum (Brevibacterium flavum) | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 208 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase Protease Serine protease |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 208 | 208 | ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444 | PRO_0000179545 | |||||
Sites | |||||||||
| Active site | 108 | 1 | By similarity | ||||||
| Active site | 133 | 1 | By similarity | ||||||
Sequences
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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. 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: BAB99804.1. BX927155 Genomic DNA. Translation: CAF21075.1. |
| RefSeq | NP_601611.1. NC_003450.3. YP_226655.1. NC_006958.1. |
3D structure databases | |
| ProteinModelPortal | Q8NN02. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S14.009. |
2D gel databases | |
| World-2DPAGE | 0001:Q8NN02. |
Proteomic databases | |
| PRIDE | Q8NN02. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1020360. 3345289. |
| GenomeReviews | Gene locus Cgl2411 in contig BA000036_GR. Gene locus cg2644 in contig BX927147_GR. |
| KEGG | cgb:cg2644. cgl:NCgl2327. |
| PATRIC | 21496826. VBICorGlu203724_2345. |
Phylogenomic databases | |
| HOGENOM | HBG558421. |
| OMA | QDPYTKL. |
| ProtClustDB | PRK12553. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627:CG2644-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00444. ClpP. [Tree] |
| InterPro | IPR023562. Pept_S14/S49. IPR001907. Pept_S14_ClpP. IPR018215. Pept_S14_ClpP_AS. [Graphical view] |
| KO | K01358. |
| PANTHER | PTHR10381. Pept_S14_ClpP. 1 hit. |
| Pfam | PF00574. CLP_protease. 1 hit. [Graphical view] |
| PRINTS | PR00127. CLPPROTEASEP. |
| PROSITE | PS00382. CLP_PROTEASE_HIS. 1 hit. PS00381. CLP_PROTEASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CLPP1_CORGL | ||||||||
| Accession | Primary (citable) accession number: Q8NN02 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with