Reviewed,
UniProtKB/Swiss-Prot Q87MK5 (CHEB1_VIBPA)
Last modified
November 3, 2009.
Version 52.
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 | Vibrio parahaemolyticus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 670 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 369 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 |
| Technical term | Complete proteome |
| 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 – 369 | 369 | Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099 | PRO_0000158038 | |||||
Regions | |||||||||
| Domain | 4 – 121 | 118 | Response regulatory | ||||||
| Domain | 176 – 369 | 194 | CheB-type methylesterase | ||||||
Sites | |||||||||
| Active site | 188 | 1 | By similarity | ||||||
| Active site | 215 | 1 | By similarity | ||||||
| Active site | 311 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 55 | 1 | 4-aspartylphosphate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 149 | 1 | S → A in AAF32418. Ref.1 | ||||||
| Sequence conflict | 170 | 1 | T → A in AAF32418. Ref.1 | ||||||
| Sequence conflict | 363 | 1 | L → M in AAF32418. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Components of the polar flagellar switch complex and assembly apparatus." Jaques S., Kim Y.K., McCarter L.L. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BB22. |
| [2] | "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6. |
Cross-references
Sequence databases | |
|---|---|
| AF069392 Genomic DNA. Translation: AAF32418.1. BA000031 Genomic DNA. Translation: BAC60491.1. | |
| RefSeq | NP_798607.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TMY based on UniProtKB Q56312. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1189741. |
| GenomeReviews | Gene locus VP2228 in contig BA000031_GR. |
| KEGG | vpa:VP2228. |
| NMPDR | fig|223926.1.peg.2228. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q87MK5. |
| OMA | WAQDEAS. |
Enzyme and pathway databases | |
| BioCyc | VPAR223926:VP2228-MON. |
| BRENDA | 3.1.1.61. 3063. |
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_VIBPA | ||||||||
| Accession | Primary (citable) accession number: Q87MK5 Secondary accession number(s): Q9LB11 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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