Q1R3B6 (CH60_ECOUT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 48.
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: 60 kDa chaperonin Alternative name(s): GroEL protein Protein Cpn60 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 364106 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 548 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions By similarity. HAMAP-Rule MF_00600 |
| Subunit structure | Oligomer of 14 subunits composed of two stacked rings of 7 subunits By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the chaperonin (HSP60) family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Chaperone |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | protein refolding 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 548 | 548 | 60 kDa chaperonin HAMAP-Rule MF_00600 | PRO_0000256909 | |||||
Amino acid modifications | |||||||||
| Modified residue | 117 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTI89 / UPEC. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | CP000243 Genomic DNA. Translation: ABE10148.1. | ||||||||||||||||||
| RefSeq | YP_543679.1. NC_007946.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q1R3B6. | ||||||||||||||||||
| SMR | Q1R3B6. Positions 2-525. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | 364106.UTI89_C4741. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q1R3B6. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | ABE10148; ABE10148; UTI89_C4741. | ||||||||||||||||||
| GeneID | 3991044. | ||||||||||||||||||
| KEGG | eci:UTI89_C4741. | ||||||||||||||||||
| PATRIC | 18458884. VBIEscCol42261_4618. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG0459. | ||||||||||||||||||
| HOGENOM | HOG000076290. | ||||||||||||||||||
| KO | K04077. | ||||||||||||||||||
| OMA | YNGVITV. | ||||||||||||||||||
| ProtClustDB | PRK00013. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | ECOL364106:GHPQ-4701-MONOMER. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_00600. CH60. | ||||||||||||||||||
| InterPro | IPR018370. Chaperonin_Cpn60_CS. IPR001844. Chaprnin_Cpn60. IPR002423. Cpn60/TCP-1. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR11353. PTHR11353. 1 hit. | ||||||||||||||||||
| Pfam | PF00118. Cpn60_TCP1. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00298. CHAPERONIN60. | ||||||||||||||||||
| SUPFAM | SSF48592. GroEL-ATPase. 1 hit. | ||||||||||||||||||
| TIGRFAMs | TIGR02348. GroEL. 1 hit. | ||||||||||||||||||
| PROSITE | PS00296. CHAPERONINS_CPN60. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | Q1R3B6. | ||||||||||||||||||
Entry information
| Entry name | CH60_ECOUT | ||||||||
| Accession | Primary (citable) accession number: Q1R3B6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
