GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
ECOLI:CHEY
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | cheY | |
| Protein Name(s) | Chemotaxis protein CheY | |
| External Links | ||
| UniProt | P0AE67 | |
| EMBL | K02175 M13463 U00096 AP009048 | |
| PIR | E25195 | |
| RefSeq | NP_416396.1 YP_490144.1 | |
| PDB | 1A0O 1AB5 1AB6 1BDJ 1C4W 1CEY 1CHN 1CYE 1D4Z 1DJM 1E6K 1E6L 1E6M 1EAY 1EHC 1F4V 1FFG 1FFS 1FFW 1FQW 1HEY 1JBE 1KMI 1MIH 1U8T 1UDR 1VLZ 1YMU 1YMV 1ZDM 2B1J 2ID7 2ID9 2IDM 2LP4 3CHY 3F7N 3FFT 3FFW 3FFX 3FGZ 3MYY 3OLV 3OLW 3OLX 3OLY 3OO0 3OO1 3RVJ 3RVK 3RVL 3RVM 3RVN 3RVO 3RVP 3RVQ 3RVR 3RVS 5CHY 6CHY | |
| PDBsum | 1A0O 1AB5 1AB6 1BDJ 1C4W 1CEY 1CHN 1CYE 1D4Z 1DJM 1E6K 1E6L 1E6M 1EAY 1EHC 1F4V 1FFG 1FFS 1FFW 1FQW 1HEY 1JBE 1KMI 1MIH 1U8T 1UDR 1VLZ 1YMU 1YMV 1ZDM 2B1J 2ID7 2ID9 2IDM 2LP4 3CHY 3F7N 3FFT 3FFW 3FFX 3FGZ 3MYY 3OLV 3OLW 3OLX 3OLY 3OO0 3OO1 3RVJ 3RVK 3RVL 3RVM 3RVN 3RVO 3RVP 3RVQ 3RVR 3RVS 5CHY 6CHY | |
| ProteinModelPortal | P0AE67 | |
| SMR | P0AE67 | |
| DIP | DIP-48237N | |
| IntAct | P0AE67 | |
| STRING | 511145.b1882 | |
| SWISS-2DPAGE | P0AE67 | |
| PaxDb | P0AE67 | |
| PRIDE | P0AE67 | |
| EnsemblBacteria | AAC74952 BAA15698 | |
| GeneID | 12930559 946393 | |
| KEGG | ecj:Y75_p1858 eco:b1882 | |
| PATRIC | 32119091 | |
| EchoBASE | EB0148 | |
| EcoGene | EG10150 | |
| eggNOG | COG0784 | |
| HOGENOM | HOG000034820 | |
| InParanoid | P0AE67 | |
| KO | K03413 | |
| OMA | MLQSGAF | |
| OrthoDB | EOG6PKFC7 | |
| PhylomeDB | P0AE67 | |
| BioCyc | EcoCyc:CHEY-MONOMER ECOL316407:JW1871-MONOMER | |
| EvolutionaryTrace | P0AE67 | |
| PRO | PR:P0AE67 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0AE67 | |
| GO | GO:0005737 GO:0016407 GO:0000287 GO:0071973 GO:0006935 GO:0018393 GO:0000160 GO:0006473 | |
| InterPro | IPR011006 IPR001789 | |
| Pfam | PF00072 | |
| SMART | SM00448 | |
| SUPFAM | SSF52172 | |
| PROSITE | PS50110 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0005737 |
cytoplasm |
ECO:0000314 |
C |
table 4 and fig 2,3,4 |
complete | |||||
| GO:0006935 |
chemotaxis |
ECO:0000021 |
P |
Figure 1. Hydrolysis of Phosphorylated CheY Phosphorylated CheY reversed flagellar rotation from CCW to CW. |
Missing: with/from | |||||
| GO:0018393 |
internal peptidyl-lysine acetylation |
ECO:0000315 |
P |
Figure 3 shows that the double-mutant with mutations in lysine residues 92 and 122 exhibits significantly less acetylation than WT. This shows that lysine 92 and 122 residues are acetylated. |
complete | |||||
| GO:0016407 |
acetyltransferase activity |
ECO:0000314 |
F |
Figure 2. CheY becomes autoacetylated when incubated with acetyl CoA; it shows autoacetyltransferase activity. |
complete | |||||
| GO:0000156 |
phosphorelay response regulator activity |
ECO:0001202 |
F |
Figure 4 (F) Involved in the transmission of sensory signals. Phosphorylated by CheA, acts as an in vivo cognate regulator for CheA in Figure 4 (F) Escherichia coli (strain K12) |
complete | |||||
|
involved_in |
GO:0018393 |
internal peptidyl-lysine acetylation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016407 |
acetyltransferase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006473 |
protein acetylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0023014 |
signal transduction by protein phosphorylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006473 |
protein acetylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000160 |
phosphorelay signal transduction system |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0071973 |
bacterial-type flagellum-dependent cell motility |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000160 |
phosphorelay signal transduction system |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
| GO:0072659 |
protein localization to plasma membrane |
ECO:0000314 |
P |
Figure 3F. shows predominant CheY chemotaxis protein localization to the cellular poles of the cell membrane. |
complete | |||||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0097588 |
archaeal or bacterial-type flagellum-dependent cell motility |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Ridgway, HG et al. (1977) Localization of proteins controlling motility and chemotaxis in Escherichia coli. J. Bacteriol. 132 657-65 PubMed GONUTS page
- ↑ Falke, JJ & Hazelbauer, GL (2001) Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26 257-65 PubMed GONUTS page
- ↑ 3.0 3.1 Liarzi, O et al. (2010) Acetylation represses the binding of CheY to its target proteins. Mol. Microbiol. 76 932-43 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 4.3 Barak, R et al. (2006) The chemotaxis response regulator CheY can catalyze its own acetylation. J. Mol. Biol. 359 251-65 PubMed GONUTS page
- ↑ Skerker, JM et al. (2005) Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol. 3 e334 PubMed GONUTS page
- ↑ Hess, JF et al. (1988) Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 53 79-87 PubMed GONUTS page
- ↑ Barak, R & Eisenbach, M (2001) Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis. Mol. Microbiol. 40 731-43 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
- ↑ Lukat, GS et al. (1990) Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis. Biochemistry 29 5436-42 PubMed GONUTS page
- ↑ 10.0 10.1 Eisenbach, M (1996) Control of bacterial chemotaxis. Mol. Microbiol. 20 903-10 PubMed GONUTS page
- ↑ Greenfield, D et al. (2009) Self-organization of the Escherichia coli chemotaxis network imaged with super-resolution light microscopy. PLoS Biol. 7 e1000137 PubMed GONUTS page
a
p
