Reviewed,
UniProtKB/Swiss-Prot O34757 (DESK_BACSU)
Last modified
January 19, 2010.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Sensor histidine kinase desK EC=2.7.13.3 | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 370 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Member of the two-component regulatory system desR/desK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates desR by phosphorylation. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 |
| Catalytic activity | ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Contains 1 histidine kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Two-component regulatory system |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein dimerization activityInferred from electronic annotation. Source: InterPro two-component sensor 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 – 370 | 370 | Sensor histidine kinase desK | PRO_0000360780 | |||||||||||||||||||||
Regions | |||||||||||||||||||||||||
| Topological domain | 1 – 10 | 10 | Extracellular Potential | ||||||||||||||||||||||
| Transmembrane | 11 – 31 | 21 | Potential | ||||||||||||||||||||||
| Topological domain | 32 – 36 | 5 | Cytoplasmic Potential | ||||||||||||||||||||||
| Transmembrane | 37 – 57 | 21 | Potential | ||||||||||||||||||||||
| Topological domain | 58 – 70 | 13 | Extracellular Potential | ||||||||||||||||||||||
| Transmembrane | 71 – 91 | 21 | Potential | ||||||||||||||||||||||
| Topological domain | 92 – 103 | 12 | Cytoplasmic Potential | ||||||||||||||||||||||
| Transmembrane | 104 – 124 | 21 | Potential | ||||||||||||||||||||||
| Topological domain | 125 – 128 | 4 | Extracellular Potential | ||||||||||||||||||||||
| Transmembrane | 129 – 149 | 21 | Potential | ||||||||||||||||||||||
| Topological domain | 150 – 370 | 221 | Cytoplasmic Potential | ||||||||||||||||||||||
| Domain | 186 – 369 | 184 | Histidine kinase | ||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||
| Modified residue | 188 | 1 | Phosphohistidine; by autocatalysis By similarity | ||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||
| Helix | 246 – 259 | 14 | |||||||||||||||||||||||
| Beta strand | 263 – 265 | 3 | |||||||||||||||||||||||
| Helix | 277 – 297 | 21 | |||||||||||||||||||||||
| Beta strand | 301 – 310 | 10 | |||||||||||||||||||||||
| Beta strand | 313 – 320 | 8 | |||||||||||||||||||||||
| Helix | 341 – 346 | 6 | |||||||||||||||||||||||
| Beta strand | 351 – 354 | 4 | |||||||||||||||||||||||
| Beta strand | 360 – 366 | 7 | |||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis." Aguilar P.S., Hernandez-Arriaga A.M., Cybulski L.E., Erazo A.C., de Mendoza D. EMBO J. 20:1681-1691(2001) [PubMed: 11285232] [Abstract] Cited for: FUNCTION. |
| [4] | "Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems." Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T., Fujita Y. J. Bacteriol. 183:7365-7370(2001) [PubMed: 11717295] [Abstract] Cited for: FUNCTION, GENE NAME. |
| [5] | "Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase." Cybulski L.E., Albanesi D., Mansilla M.C., Altabe S., Aguilar P.S., de Mendoza D. Mol. Microbiol. 45:1379-1388(2002) [PubMed: 12207704] [Abstract] Cited for: FUNCTION. |
| [6] | "Genetic evidence for the temperature-sensing ability of the membrane domain of the Bacillus subtilis histidine kinase DesK." Hunger K., Beckering C.L., Marahiel M.A. FEMS Microbiol. Lett. 230:41-46(2004) [PubMed: 14734164] [Abstract] Cited for: FUNCTION. |
| [7] | "The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator." Albanesi D., Mansilla M.C., de Mendoza D. J. Bacteriol. 186:2655-2663(2004) [PubMed: 15090506] [Abstract] Cited for: FUNCTION. |
| [8] | "The Bacillus subtilis desaturase: a model to understand phospholipid modification and temperature sensing." Mansilla M.C., de Mendoza D. Arch. Microbiol. 183:229-235(2005) [PubMed: 15711796] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF027868 Genomic DNA. Translation: AAB84437.1. AL009126 Genomic DNA. Translation: CAB13811.1. | ||||||||||||||||||||||||||||||||||||||||||||||||
| PIR | C69901. | ||||||||||||||||||||||||||||||||||||||||||||||||
| RefSeq | NP_389800.1. | ||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| GeneID | 939678. | ||||||||||||||||||||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus BSU19190 in contig AL009126_GR. | ||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG | bsu:BSU19190. | ||||||||||||||||||||||||||||||||||||||||||||||||
| NMPDR | fig|224308.1.peg.1923. | ||||||||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| SubtiList | BG13519. desK. [Micado] | ||||||||||||||||||||||||||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| HOGENOM | HBG700937. | ||||||||||||||||||||||||||||||||||||||||||||||||
| OMA | LESTASM. | ||||||||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| BioCyc | SUBTI:BSU19190-MONOMER. | ||||||||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR003594. ATPase-like_ATP-bd. IPR011712. Sig_transdc_His_kin_sub3_dim/P. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF02518. HATPase_c. 1 hit. PF07730. HisKA_3. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||
| SMART | SM00387. HATPase_c. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||
| PROSITE | PS50109. HIS_KIN. False negative. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | DESK_BACSU | ||||||||
| Accession | Primary (citable) accession number: O34757 Secondary accession number(s): Q796C8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


