Q8Q009 (CHEB1_METMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 60.
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 response regulator protein-glutamate methylesterase of group 1 operon EC=3.1.1.61 | ||||
| Gene names |
| ||||
| Organism | Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 192952 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
Protein attributes
| Sequence length | 357 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_00099 |
| 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. HAMAP MF_00099 |
| 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: UniProtKB-KW regulation of transcription, DNA-dependentInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein-glutamate methylesterase activity Inferred from electronic annotation. Source: EC 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 – 357 | 357 | Chemotaxis response regulator protein-glutamate methylesterase of group 1 operon HAMAP MF_00099 | PRO_0000158053 | |||||
Regions | |||||||||
| Domain | 10 – 127 | 118 | Response regulatory | ||||||
| Domain | 159 – 353 | 195 | CheB-type methylesterase | ||||||
Sites | |||||||||
| Active site | 171 | 1 | By similarity | ||||||
| Active site | 198 | 1 | By similarity | ||||||
| Active site | 295 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 61 | 1 | 4-aspartylphosphate By similarity | ||||||
Sequences
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References
| [1] | "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. Gottschalk G.J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008384 Genomic DNA. Translation: AAM30025.1. |
| RefSeq | NP_632353.2. NC_003901.1. |
3D structure databases | |
| ProteinModelPortal | Q8Q009. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1478671. |
| GenomeReviews | Gene locus MM_0329 in contig AE008384_GR. |
| KEGG | mma:MM_0329. |
| NMPDR | fig|192952.1.peg.329. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG705324. |
| OMA | ILIDEDM. |
| PhylomeDB | Q8Q009. |
| ProtClustDB | PRK00742. |
Enzyme and pathway databases | |
| BioCyc | MMAZ192952:MM0329-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00099. CheB_methylest. [Tree] |
| InterPro | IPR011006. CheY-like_superfamily. 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. |
| KO | K03412. |
| Pfam | PF01339. CheB_methylest. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view] |
| PIRSF | PIRSF000876. RR_chemtxs_CheB. 1 hit. |
| SMART | SM00448. REC. 1 hit. [Graphical view] |
| SUPFAM | SSF52738. Chemotax_RR_pGlu_Me-esterase. 1 hit. SSF52172. CheY_like. 1 hit. |
| PROSITE | PS50122. CHEB. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHEB1_METMA | ||||||||
| Accession | Primary (citable) accession number: Q8Q009 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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