Summary: CheD chemotactic sensory transduction
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CheD chemotactic sensory transduction Provide feedback
This chemotaxis protein stimulates methylation of MCP proteins [1]. The chemotaxis machinery of Bacillus subtilis is similar to that of the well characterised system of Escherichia coli. However, B. subtilis contains several chemotaxis genes not found in the E. coli genome, such as CheC and CheD, indicating that the B. subtilis chemotactic system is more complex. CheD plays an important role in chemotactic sensory transduction for many organisms. CheD deamidates other B. subtilis chemoreceptors including McpB and McpC. Deamidation by CheD is required for B. subtilis chemoreceptors to effectively transduce signals to the CheA kinase [2]. The structure of a complex between the signal-terminating phosphatase, CheC, and the receptor-modifying deamidase, CheD, reveals how CheC mimics receptor substrates to inhibit CheD and how CheD stimulates CheC phosphatase activity. CheD resembles other cysteine deamidases from bacterial pathogens that inactivate host Rho-GTPases. Phospho-CheY, the intracellular signal and CheC target, stabilises the CheC-CheD complex and reduces availability of CheD [3]. A model is proposed whereby CheC acts as a CheY-P-induced regulator of CheD; CheY-P would cause CheC to sequester CheD from the chemoreceptors, inducing adaptation of the chemotaxis system [4].
Literature references
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Rosario MM, Ordal GW; , Mol Microbiol 1996;21:511-518.: CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins. PUBMED:8866475 EPMC:8866475
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Kristich CJ, Ordal GW;, J Biol Chem. 2002;277:25356-25362.: Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis. PUBMED:12011078 EPMC:12011078
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Chao X, Muff TJ, Park SY, Zhang S, Pollard AM, Ordal GW, Bilwes AM, Crane BR;, Cell. 2006;124:561-571.: A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation. PUBMED:16469702 EPMC:16469702
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Muff TJ, Ordal GW;, J Biol Chem. 2007;282:34120-34128.: The CheC phosphatase regulates chemotactic adaptation through CheD. PUBMED:17908686 EPMC:17908686
External database links
| PANDIT: | PF03975 |
| Pseudofam: | PF03975 |
| SYSTERS: | CheD |
This tab holds annotation information from the InterPro database.
InterPro entry IPR005659
CheD deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the cheA kinase [PUBMED:17908686]. CheC is a CheY-P phosphatase (CheY controls flagellar rotation and is activated by phosphorylation). The activity of CheC is enhanced by its interaction with CheD, forming a CheC-CheD heterodimer. It is suggested that CheC exerts its effect on MCP methylation in Bacillus subtilis by controlling the binding of CheD to the MCPs [PUBMED:8866475].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | protein-glutamine glutaminase activity (GO:0050568) |
| Biological process | chemotaxis (GO:0006935) |
Domain organisation
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Alignments
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| Seed (150) |
Full (1074) |
Representative proteomes | NCBI (920) |
Meta (66) |
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| RP15 (151) |
RP35 (288) |
RP55 (351) |
RP75 (412) |
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| PP/heatmap | 1 | |||||||
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| Seed (150) |
Full (1074) |
Representative proteomes | NCBI (920) |
Meta (66) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (151) |
RP35 (288) |
RP55 (351) |
RP75 (412) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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Trees
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Curation and family details
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Curation
| Seed source: | COG1871 |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 150 |
| Number in full: | 1074 |
| Average length of the domain: | 114.90 aa |
| Average identity of full alignment: | 30 % |
| Average coverage of the sequence by the domain: | 61.85 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 114 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CheD domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence