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20  structures 2027  species 2  interactions 5059  sequences 27  architectures

Clan: CheC-like (CL0355)

Summary

CheC-like superfamily Add an annotation

The chemotactic response regulator superfamily are CheY-P phosphatases. Their structure is two intertwined alpha-beta-(X)-beta(2) motifs. This superfamily comprises two classes of proteins each shown to interact with the chemotaxis response regulator CheY: the FliM switch proteins and the CheC-type phosphatases [1]. FliM is a component of the flagellar switch found across the bacteria and is responsible for binding CheY-P and changing the rotational direction of the flagella. The N-terminal domain is CheC-like and the C-terminal shares the SpoA domain with FliN and FliY. The CheC family is broadly broken down into three phosphatase subfamilies: CheC, CheX, and FliY. All three have an active site consensus sequence of D/S-X(3)-E-X(2)-N-X(22)-P.

This clan contains 4 families and the total number of domains in the clan is 5059. The clan was built by A Bateman and TJ Tuff.

Literature references

  1. Muff TJ, Ordal GW;, Mol Microbiol. 2008;70:1054-1061.: The diverse CheC-type phosphatases: chemotaxis and beyond. PUBMED:18990184 EPMC:18990184

Members

This clan contains the following 4 member families:

CheC CheX DUF3334 FliM

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
FliM (PF02154) 1999 (39.5%) View
CheC (PF04509) 1993 (39.4%) View
CheX (PF13690) 880 (17.4%) View
DUF3334 (PF11813) 187 (3.7%) View
Total: 4 Total: 5059 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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Interactions

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

Interacting families
A B
CheC 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 MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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