P0AE68 (CHEY_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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: Chemotaxis protein CheY | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 129 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation By similarity. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available By similarity. |
| Sequence similarities | Contains 1 response regulatory domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Chemotaxis Flagellar rotation Two-component regulatory system |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW ciliary or flagellar motilityInferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependentInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW two-component response regulator activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 129 | 128 | Chemotaxis protein CheY | PRO_0000081041 | |||||
Regions | |||||||||
| Domain | 7 – 124 | 118 | Response regulatory | ||||||
Sites | |||||||||
| Metal binding | 12 | 1 | Magnesium By similarity | ||||||
| Metal binding | 13 | 1 | Magnesium By similarity | ||||||
| Metal binding | 57 | 1 | Magnesium By similarity | ||||||
| Metal binding | 59 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 57 | 1 | 4-aspartylphosphate By similarity | ||||||
| Modified residue | 92 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 109 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG56872.1. BA000007 Genomic DNA. Translation: BAB36015.1. |
| PIR | D85801. H90952. |
| RefSeq | NP_288319.1. NC_002655.2. NP_310619.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0AE68. |
| SMR | P0AE68. Positions 2-129. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-98475. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000024252; EBESCP00000023145; EBESCG00000023306. EBESCT00000059093; EBESCP00000056921; EBESCG00000058141. |
| GeneID | 914203. 961854. |
| GenomeReviews | Gene locus Z2936 in contig AE005174_GR. Gene locus ECs2592 in contig BA000007_GR. |
| KEGG | ece:Z2936. ecs:ECs2592. |
| PATRIC | 18354562. VBIEscCol44059_2492. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000008654. |
| HOGENOM | HBG753323. |
| OMA | GFTNTSE. |
| ProtClustDB | PRK10610. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS2592-MONOMER. |
Family and domain databases | |
| InterPro | IPR011006. CheY-like_superfamily. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view] |
| KO | K03413. |
| Pfam | PF00072. Response_reg. 1 hit. [Graphical view] |
| SMART | SM00448. REC. 1 hit. [Graphical view] |
| SUPFAM | SSF52172. CheY_like. 1 hit. |
| PROSITE | PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHEY_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AE68 Secondary accession number(s): P06143 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with