Reviewed,
UniProtKB/Swiss-Prot O52262 (CHEB1_PSEPU)
Last modified
June 16, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon EC=3.1.1.61 | ||
| Gene names |
| ||
| Organism | Pseudomonas putida | ||
| Taxonomic identifier | 303 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 374 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by cheR By similarity. |
| Catalytic activity | Protein L-glutamate O(5)-methyl ester + H2O = protein L-glutamate + methanol. HAMAP MF_00099 |
| Subcellular location | |
| Domain | The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain. HAMAP MF_00099 |
| Post-translational modification | Phosphorylated by cheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain By similarity. |
| Sequence similarities | Contains 1 cheB-type methylesterase domain. Contains 1 response regulatory domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Chemotaxis |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | chemotaxis Inferred from electronic annotation. Source: HAMAP regulation of transcription, DNA-dependentInferred from electronic annotation. Source: InterPro sensory perception of chemical stimulusInferred from electronic annotation. Source: HAMAP two-component signal transduction system (phosphorelay)Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein-glutamate methylesterase activity Inferred from electronic annotation. Source: HAMAP 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 374 | 374 | Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099 | PRO_0000158013 | |||||
Regions | |||||||||
| Domain | 4 – 121 | 118 | Response regulatory | ||||||
| Domain | 183 – 374 | 192 | CheB-type methylesterase | ||||||
Sites | |||||||||
| Active site | 198 | 1 | By similarity | ||||||
| Active site | 225 | 1 | By similarity | ||||||
| Active site | 318 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 55 | 1 | 4-aspartylphosphate By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 141 – 147 | 7 | RPAPVAA → LAGAGRR in MK1. HAMAP MF_00099 | ||||||
| Natural variant | 193 – 194 | 2 | VA → LR in MK1. HAMAP MF_00099 | ||||||
Sequences
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References
| [1] | "Identification of a chemotaxis gene region from Pseudomonas putida." Ditty J.L., Grimm A.C., Harwood C.S. FEMS Microbiol. Lett. 159:267-273(1998) [PubMed: 9503621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PRS2000. |
| [2] | "The G-protein FlhF has a role in polar flagellar placement and general stress response induction in Pseudomonas putida." Pandza S., Baetens M., Park C.H., Au T., Keyhan M., Matin A. Mol. Microbiol. 36:414-423(2000) [PubMed: 10792727] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MK1. |
Cross-references
Sequence databases | |
|---|---|
| AF031898 Genomic DNA. Translation: AAC08065.1. AF183382 Genomic DNA. Translation: AAF67048.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CHD based on UniProtKB P04042. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.61. 403. |
Family and domain databases | |
| HAMAP | MF_00099. [Tree] |
| InterPro | IPR008248. Sig_transdc_resp-reg_CheB. IPR000673. Sig_transdc_resp-reg_Me-estase. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view] |
| Gene3D | G3DSA:3.40.50.180. Chemotax_RR_pGlu_Me-esterase. 1 hit. |
| Pfam | PF01339. CheB_methylest. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view] |
| PIRSF | PIRSF000876. RR_chemtxs_CheB. 1 hit. |
| ProDom | PD005328. CheB_methylest. 1 hit. PD000039. Response_reg. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00448. REC. 1 hit. [Graphical view] |
| PROSITE | PS50122. CHEB. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHEB1_PSEPU | ||||||||
| Accession | Primary (citable) accession number: O52262 Secondary accession number(s): Q9L942 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


