Reviewed,
UniProtKB/Swiss-Prot P0AEC8 (DCUS_ECOLI)
Last modified
June 16, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Sensor protein dcuS EC=2.7.13.3 | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 543 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Member of the two-component regulatory system dcuR/dcuS. Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-dicarboxylate transporter dctA. Activates dcuR by phosphorylation. |
| Catalytic activity | ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. |
| Enzyme regulation | Autophosphorylation is stimulated by the presence of fumarate or succinate. |
| Subcellular location | |
| Post-translational modification | Autophosphorylated. The phosphoryl group is rapidely transferred to dcuR. |
| Miscellaneous | The region encompassing approximately residues 42 to 181 has been shown to be periplasmic, however exactly which residues are periplasmic is not clear. |
| Sequence similarities | Contains 1 histidine kinase domain. Contains 1 PAS (PER-ARNT-SIM) domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 543 | 543 | Sensor protein dcuS | PRO_0000074750 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Topological domain | 1 – 20 | 20 | Cytoplasmic Potential | ||||||||||||||||||||||||||||||||||
| Transmembrane | 21 – 41 | 21 | Potential | ||||||||||||||||||||||||||||||||||
| Topological domain | 42 – 181 | 140 | Periplasmic Potential | ||||||||||||||||||||||||||||||||||
| Transmembrane | 182 – 202 | 21 | Potential | ||||||||||||||||||||||||||||||||||
| Topological domain | 203 – 543 | 341 | Cytoplasmic Potential | ||||||||||||||||||||||||||||||||||
| Domain | 220 – 291 | 72 | PAS | ||||||||||||||||||||||||||||||||||
| Domain | 346 – 538 | 193 | Histidine kinase | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 349 | 1 | Phosphohistidine; by autocatalysis By similarity | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Helix | 46 – 63 | 18 | |||||||||||||||||||||||||||||||||||
| Helix | 68 – 73 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 77 – 79 | 3 | |||||||||||||||||||||||||||||||||||
| Turn | 82 – 84 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 85 – 93 | 9 | |||||||||||||||||||||||||||||||||||
| Beta strand | 97 – 104 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 113 | 3 | |||||||||||||||||||||||||||||||||||
| Turn | 114 – 117 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 125 – 128 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 138 | 5 | |||||||||||||||||||||||||||||||||||
| Turn | 141 – 143 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 145 – 153 | 9 | |||||||||||||||||||||||||||||||||||
| Beta strand | 155 – 157 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 159 – 167 | 9 | |||||||||||||||||||||||||||||||||||
| Helix | 173 – 178 | 6 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [2] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system." Zientz E., Bongaerts J., Unden G. J. Bacteriol. 180:5421-5425(1998) [PubMed: 9765574] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
| [5] | "Identification and characterization of a two-component sensor-kinase and response-regulator system (DcuS-DcuR) controlling gene expression in response to C4-dicarboxylates in Escherichia coli." Golby P., Davies S., Kelly D.J., Guest J.R., Andrews S.C. J. Bacteriol. 181:1238-1248(1999) [PubMed: 9973351] [Abstract] Cited for: CHARACTERIZATION, TOPOLOGY. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
| [6] | "Function of DcuS from Escherichia coli as a fumarate-stimulated histidine protein kinase in vitro." Janausch I.G., Garcia-Moreno I., Unden G. J. Biol. Chem. 277:39809-39814(2002) [PubMed: 12167640] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / AN387. |
| [7] | "Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U14003 Genomic DNA. Translation: AAA97025.1. U00096 Genomic DNA. Translation: AAC77086.1. AP009048 Genomic DNA. Translation: BAE78127.1. | |||||||||||||||||||||||||
| PIR | D65222. | ||||||||||||||||||||||||
| RefSeq | AP_004626.1. NP_418549.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P0AEC8. 1 interaction. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| GeneID | 948639. | ||||||||||||||||||||||||
| GenomeReviews | Gene locus JW4086 in contig AP009048_GR. Gene locus b4125 in contig U00096_GR. | ||||||||||||||||||||||||
| KEGG | ecj:JW4086. eco:b4125. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| EchoBASE | EB2358. | ||||||||||||||||||||||||
| EcoGene | EG12465. dcuS. | ||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P0AEC8. | ||||||||||||||||||||||||
| OMA | P0AEC8. RNTMLQS. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | EcoCyc:DCUS-MON. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR003594. ATP_bd_ATPase. IPR000014. PAS. IPR013767. PAS_fold. IPR004358. Sig_transdc_His_kin-like_C. IPR005467. Sig_transdc_His_kinase_core. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF02518. HATPase_c. 1 hit. PF00989. PAS. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR00344. BCTRLSENSOR. | ||||||||||||||||||||||||
| SMART | SM00387. HATPase_c. 1 hit. SM00091. PAS. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| TIGRFAMs | TIGR00229. sensory_box. 1 hit. | ||||||||||||||||||||||||
| PROSITE | PS50109. HIS_KIN. 1 hit. PS50112. PAS. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | DCUS_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0AEC8 Secondary accession number(s): P39272, P76795, Q2M6H9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


