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2  structures 935  species 2  interactions 1074  sequences 8  architectures

Family: CheD (PF03975)

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

  1. 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

  2. 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

  3. 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

  4. 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

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

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Domain organisation

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Alignments

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Full
(1074)
Representative proteomes NCBI
(920)
Meta
(66)
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(151)
RP35
(288)
RP55
(351)
RP75
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  Seed
(150)
Full
(1074)
Representative proteomes NCBI
(920)
Meta
(66)
RP15
(151)
RP35
(288)
RP55
(351)
RP75
(412)
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  Seed
(150)
Full
(1074)
Representative proteomes NCBI
(920)
Meta
(66)
RP15
(151)
RP35
(288)
RP55
(351)
RP75
(412)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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Curation and family details

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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 View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 34.3 27.9
Noise cut-off 21.8 21.4
Model length: 114
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

CheD CheC

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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