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9  structures 3908  species 0  interactions 9409  sequences 386  architectures

Family: CheB_methylest (PF01339)

Summary: CheB methylesterase

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This is the Wikipedia entry entitled "Protein-glutamate methylesterase". More...

Protein-glutamate methylesterase Edit Wikipedia article

In enzymology, a protein-glutamate methylesterase (EC is an enzyme that catalyzes the chemical reaction

protein L-glutamate O5-methyl ester + H2O protein L-glutamate + methanol

Thus, the two substrates of this enzyme are protein L-glutamate O5-methyl ester and H2O, whereas its two products are protein L-glutamate and methanol.

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is protein-L-glutamate-O5-methyl-ester acylhydrolase. Other names in common use include chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, CheB methylesterase, methylesterase CheB, protein methyl-esterase, protein carboxyl methylesterase, PME, protein methylesterase, and protein-L-glutamate-5-O-methyl-ester acylhydrolase. This enzyme participates in 3 metabolic pathways: two-component system - general, bacterial chemotaxis - general, and bacterial chemotaxis - organism-specific.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1A2O and 1CHD.


Template:Enzyme references

  • Gagnon C, Harbour D, Camato R (1984). "Purification and characterization of protein methylesterase from rat kidney". J. Biol. Chem. 259: 10212–5. PMID 6469959.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Kehry MR, Doak TG, Dahlquist FW (1984). "Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli". J. Biol. Chem. 259: 11828–35. PMID 6384215.{{cite journal}}: CS1 maint: multiple names: authors list (link)

External links

The CAS registry number for this enzyme class is Template:CAS registry.

Template:Enzyme links

Gene Ontology (GO) codes

Template:GO code links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

CheB methylesterase Provide feedback

No Pfam abstract.

Literature references

  1. West AH, Martinez-Hackert E, Stock AM; , J Mol Biol 1995;250:276-290.: Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB. PUBMED:7608974 EPMC:7608974

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000673

Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ PUBMED:16176121 ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ PUBMED:18076326 ]. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more [ PUBMED:12372152 ]. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) [ PUBMED:10966457 ]. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.

A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [ PUBMED:11934609 , PUBMED:11489844 ].

This entry represents the signal transduction response regulator CheB involved in chemotaxis. CheB methylesterase is responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). The enzyme catalyses the reaction: protein L-glutamate O-methyl ester and water is converted to protein L-glutamate and methanol. CheB is regulated through phosphorylation by CheA. The N-terminal region of the protein is similar to that of other regulatory components of sensory transduction systems. The Myxococcus xanthus FrzG protein also belongs to this family, and is required for the normal aggregation of cells during fruiting body formation.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Sarah Teichmann
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A
Number in seed: 879
Number in full: 9409
Average length of the domain: 176.2 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 35.34 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.6 22.6
Trusted cut-off 22.7 22.8
Noise cut-off 22.4 22.5
Model length: 168
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 CheB_methylest domain has been found. There are 9 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A1SMR4 View 3D Structure Click here
B2J4Q8 View 3D Structure Click here
G3XD63 View 3D Structure Click here
O29221 View 3D Structure Click here
O51376 View 3D Structure Click here
O83639 View 3D Structure Click here
O85128 View 3D Structure Click here
O87125 View 3D Structure Click here
O87717 View 3D Structure Click here
P04042 View 3D Structure Click here
P07330 View 3D Structure Click here
P0DMI2 View 3D Structure Click here
P62635 View 3D Structure Click here
P62636 View 3D Structure Click here
P62637 View 3D Structure Click here
P62638 View 3D Structure Click here
P62639 View 3D Structure Click here
P62640 View 3D Structure Click here
P62644 View 3D Structure Click here
P62645 View 3D Structure Click here
P62646 View 3D Structure Click here
P62647 View 3D Structure Click here
P72253 View 3D Structure Click here
Q05522 View 3D Structure Click here
Q085K9 View 3D Structure Click here
Q0A9Z5 View 3D Structure Click here
Q0ARY3 View 3D Structure Click here
Q0AWZ8 View 3D Structure Click here
Q0AXB7 View 3D Structure Click here
Q0AYL3 View 3D Structure Click here
Q0P9X5 View 3D Structure Click here
Q10WZ6 View 3D Structure Click here
Q12IZ9 View 3D Structure Click here
Q12PJ3 View 3D Structure Click here
Q12YX1 View 3D Structure Click here
Q13SY2 View 3D Structure Click here
Q15RF6 View 3D Structure Click here
Q167K9 View 3D Structure Click here
Q1CWZ9 View 3D Structure Click here
Q1CX06 View 3D Structure Click here