C2GTS9 (C2GTS9_BIFLN) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 16.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444 EC=3.4.21.92 HAMAP MF_00444 Alternative name(s): Endopeptidase Clp 2 HAMAP MF_00444 | ||||
| Gene names |
| ||||
| Organism | Bifidobacterium longum subsp. longum ATCC 55813 EMBL EEI81486.1 | ||||
| Taxonomic identifier | 548480 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium |
Protein attributes
| Sequence length | 207 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. RuleBase RU003567 HAMAP MF_00444 |
| Caution | The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm HAMAP MF_00444 |
| Ligand | ATP-binding HAMAP MF_00444 Nucleotide-binding |
| Molecular function | Hydrolase Protease Serine protease HAMAP MF_00444 |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: HAMAP |
| 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 102 | 1 | By similarity HAMAP MF_00444 | ||||||
| Active site | 127 | 1 | By similarity HAMAP MF_00444 | ||||||
Sequences
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References
| [1] | Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. Gibbs R.Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 55813 EMBL EEI81486.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ACHI01000008 Genomic DNA. Translation: EEI81486.1. |
3D structure databases | |
| ProteinModelPortal | C2GTS9. |
| SMR | C2GTS9. Positions 23-196. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 36941652. VBIBifLon7869_0418. |
Family and domain databases | |
| HAMAP | MF_00444. ClpP. [Tree] |
| InterPro | IPR023562. Pept_S14/S49. IPR001907. Pept_S14_ClpP. [Graphical view] |
| PANTHER | PTHR10381. Pept_S14_ClpP. 1 hit. |
| Pfam | PF00574. CLP_protease. 1 hit. [Graphical view] |
| PRINTS | PR00127. CLPPROTEASEP. |
| ProtoNet | Search... |
Entry information
| Entry name | C2GTS9_BIFLN | ||||||||
| Accession | Primary (citable) accession number: C2GTS9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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